"{{c1::K<sub>m</sub>}}&nbsp;is the <u>substrate concentration</u> that gives you a reaction<i> </i>rate that is<i>&nbsp;halfway to V<sub style="""">max</sub></i>""<div><img src=""Km and Vmax.png"" style=""vertical-align: sub;""></div><div><br></div><div><a href=""https://www.khanacademy.org/science/biology/energy-and-enzymes/enzyme-regulation/a/basics-of-enzyme-kinetics-graphs"">Khan Academy Link</a><br></div>"MileDown::Biochemistry::Enzymes::Kinetics
"<div>The <b>Michaelis–Menten equation</b> is:</div><div><br></div><div>{{c1::<img src=""Michalis Menten Equation.png"">}}</div>""<div><a href=""https://www.khanacademy.org/test-prep/mcat/biomolecules/enzyme-kinetics/v/steady-states-and-the-michaelis-menten-equation"">Khan Academy Link</a><br></div>"MileDown::Biochemistry::Enzymes::Kinetics
{{c1::Cooperative binding}} is when the binding of the first molecule of B to A <i>changes the binding affinity</i> of the second B molecule, making it more or less likely to bind"<div>Results in a sigmoidal curve</div><div><br></div><div><div><img src=""Cooperative Binding Curve.png""></div><div><br></div><div><a href=""https://www.khanacademy.org/test-prep/mcat/biomolecules/enzyme-kinetics/v/cooperativity"">Khan Academy Link</a></div></div>"MileDown::Biochemistry::Enzymes::Kinetics
<div><div>A/an {{c1::competitive inhibitor::... inhibitor}} <i>binds at the&nbsp;active site</i>&nbsp;and thus prevents the&nbsp;substrate from binding&nbsp;</div></div>"<div>Can be overcome by adding more substrate<br></div><div><br></div><div><img src=""Inhibition (1).png""></div><div><br></div><div><a href=""https://www.khanacademy.org/science/biology/energy-and-enzymes/enzyme-regulation/v/competitive-inhibition"">Khan Academy Link</a></div>"MileDown::Biochemistry::Enzymes::Regulation
<div>A/an {{c1::uncompetitive inhibitor::... inhibitor}} binds only with the&nbsp;<u>enzyme-substrate&nbsp;complex</u></div>"<div><img src=""Inhibition (1).png""></div><div><br></div><div><a href=""https://www.khanacademy.org/test-prep/mcat/biomolecules/enzyme-kinetics/v/enzymatic-inhibition-and-lineweaver-burke-plots"">Khan Academy Link</a><br></div>"MileDown::Biochemistry::Enzymes::Regulation
A/an {{c1::noncompetitive inhibitor::... inhibitor}} <b>binds at the&nbsp;allosteric site</b>, away from the active site"<div>It does <i>not</i> prevent the substrate from&nbsp;binding to the active site<br></div><div><br></div><div><img src=""Inhibition (1).png""></div><div><br></div><div><a href=""https://www.khanacademy.org/science/biology/energy-and-enzymes/enzyme-regulation/v/noncompetitive-inhibition"">Khan Academy Link</a></div>"MileDown::Biochemistry::Enzymes::Regulation
In <i>competitive inhibition</i>:<div><br></div><div>V<sub>max</sub>: {{c1::has no change}}</div><div>K<sub>m</sub>: {{c1::goes up}}</div>"<div><img src=""Inhibition (1).png""></div><div><br></div><div><a href=""https://www.khanacademy.org/science/biology/energy-and-enzymes/enzyme-regulation/v/competitive-inhibition"">Khan Academy Link</a></div>"MileDown::Biochemistry::Enzymes::Regulation
In&nbsp;<u>uncompetitive inhibition</u>:<div><br></div><div><div>V<sub>max</sub>: {{c1::goes down}}</div><div>K<sub>m</sub>: {{c1::goes down}}</div></div>"<div><img src=""Inhibition (1).png""></div><div><br></div><div><a href=""https://www.khanacademy.org/test-prep/mcat/biomolecules/enzyme-kinetics/v/enzymatic-inhibition-and-lineweaver-burke-plots"">Khan Academy Link</a></div>"MileDown::Biochemistry::Enzymes::Regulation
In&nbsp;<b>noncompetitive inhibition</b>:<div><br></div><div><div>V<sub>max</sub>: {{c1::goes down}}</div><div>K<sub>m</sub>: {{c1::has no change}}</div></div>"<div><img src=""Inhibition (1).png""></div><div><br></div><div><a href=""https://www.khanacademy.org/science/biology/energy-and-enzymes/enzyme-regulation/v/noncompetitive-inhibition"">Khan Academy Link</a></div>"MileDown::Biochemistry::Enzymes::Regulation
"<img src=""Lineweaver Burk.png""><div><br><div><u>Lineweaver-Burk Plot</u>:&nbsp;</div><div><br></div><div>X-intercept = {{c1::-1/K<sub>m</sub>}}</div><div>Y-intercept = {{c1::1/V<sub>max</sub>}}</div><div>Ratio indicated by the slope = {{c1::K<sub>m</sub>/V<sub>max</sub>}}<br></div></div>""<img src=""Lineweaver Burk Complete.png""><div><br></div><div><a href=""https://www.youtube.com/watch?v=GVUkZL1jCw0&quot;"">YouTube Link</a></div>"MileDown::Biochemistry::Enzymes::Regulation
"<img src=""Lineweaver Burk Competitive .png""><div><br></div><div>This graph shows the activity of a/an {{c1::competitive inhibitor::... inhibitor}}</div>""<img src=""Lineweaver Burk All.png""><div><br></div><div><a href=""https://www.youtube.com/watch?v=GVUkZL1jCw0"" ""="""">YouTube Link</a></div>"MileDown::Biochemistry::Enzymes::Regulation
"<img src=""Lineweaver Burk Uncompetitive.png""><div><br><div>This graph shows the activity of a/an {{c1::uncompetitive inhibitor::... inhibitor}}</div></div>""<img src=""Lineweaver Burk All.png""><div><br></div><div><a href=""https://www.youtube.com/watch?v=GVUkZL1jCw0"" ""="""">YouTube Link</a></div>"MileDown::Biochemistry::Enzymes::Regulation
"<img src=""Lineweaver Burk Noncompetitive .png""><div><br><div>This graph shows the activity of a/an {{c1::noncompetitive inhibitor::... inhibitor}}</div></div>""<img src=""Lineweaver Burk All.png""><div><br></div><div><a href=""https://www.youtube.com/watch?v=GVUkZL1jCw0"" ""="""">YouTube Link</a><br></div>"MileDown::Biochemistry::Enzymes::Regulation
<div>An <i>irreversible inhibitor</i>&nbsp;is any inhibitor that&nbsp;{{c1::covalently binds}}&nbsp;to the active site of some enzyme, thus eliminating its activity</div>"<div><img src=""Irreversible Inhibition.png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=ixDdTbeby6s"">YouTube Link</a><br></div>"MileDown::Biochemistry::Enzymes::Regulation
<div>The <b>binding of oxygen<sub>&nbsp;</sub>to&nbsp;hemoglobin</b> can be characterized as {{c1::cooperative}}</div>"<div>When one O<sub style="""">2</sub>&nbsp;molecule binds to one of the four heme groups in a hemoglobin, <i>it becomes more&nbsp;likely</i> that the remaining sites will bind to O<sub style="""">2</sub></div><div><sub style=""""><br></sub></div><div><sub><img src=""Hemoglobin and Myoglobin Dissociation Curves.png""></sub></div><div><sub><br></sub></div><div><a href=""https://www.khanacademy.org/science/health-and-medicine/advanced-hematologic-system/hematologic-system-introduction/v/hemoglobin-moves-o2-and-co2"">Khan Academy Link</a><br></div>"MileDown::Biology::Cardiovascular_System
{{c1::P<sub>50</sub>}}&nbsp;is the <b>oxygen pressure</b> when&nbsp;<u>50% of hemoglobin/myoglobin have an oxygen&nbsp;bound</u>"<div><img src=""P50.png""></div><div><br></div><div><a href=""https://youtu.be/HYbvwMSzqdY"">YouTube Link</a><br></div>"MileDown::Biology::Cardiovascular_System
<u>Myoglobin</u> stores and releases oxygen in&nbsp;{{c1::muscle tissue}}"<div><i>Not pH sensitive</i></div><div><font color=""#e12727""><br></font></div><div><font color=""#e12727""><img src=""Myoglobin Curve.jpg""></font></div><div><font color=""#e12727""><br></font></div><div><a href=""https://www.youtube.com/watch?v=XUI5vGfNYZY"">YouTube Link</a><br></div>"MileDown::Biology::Cardiovascular_System MileDown::Biology::Muscular_System
"<img src=""Fate of Pyruvate 1.png""><div><br></div><div>The 3 compounds that <b style="""">pyruvate will convert</b><i> </i><b>to</b> are {{c1::acetaldehyde}}, {{c1::lactate}}, and {{c1::acetyl-CoA}}</div>""<div><img src=""Fate of Pyruvate.png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=It4j3sdz9R4"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Glycolysis
"<img src=""Fate of Pyruvate 3.png""><div><br></div><div>When <b>pyruvate</b> converts to <i>acetaldehyde</i>, the next step converts acetaldehyde to {{c1::ethanol}}</div>""<div><img src=""Fate of Pyruvate.png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=It4j3sdz9R4"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Glycolysis
"<img src=""Acetyl CoA Fate.png""><div><br></div><div><i>Acetyl-CoA</i> feeds into the following two processes:</div><div><br></div><div>{{c1::Citric acid cycle}}</div><div><br></div><div>{{c1::Fatty acid synthesis}}</div>""<div><img src=""Acetyl CoA Fate Complete.png""></div><div><br></div><div><a href=""https://www.khanacademy.org/test-prep/mcat/biomolecules/fat-and-protein-metabolism/v/fatty-acid-synthesis-part-i"">Khan Academy Link - Fatty Acid Synthesis</a><br></div><div><a href=""https://www.khanacademy.org/science/biology/cellular-respiration-and-fermentation/pyruvate-oxidation-and-the-citric-acid-cycle/v/krebs-citric-acid-cycle"">Khan Academy Link - Citric Acid Cycle</a><br></div>"MileDown::Biochemistry::Metabolism::Acetyl-CoA
"<img src=""Electron Transport Chain.png""><div><br></div><div>The <u>citric acid cycle</u> sends electrons to the {{c1::electron transport chain}}</div>""<div>The electron transport chain converts <i>ADP to ATP</i></div><div><br></div><div><img src=""Electron Transport Chain Complete.png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=C8VHyezOJD4"">YouTube Link</a></div>"MileDown::Biochemistry::Metabolism::ETC
The three major regulatory enzymes in <u>glycolysis</u> are:<div><br></div><div><div>{{c1::Hexokinase (Step 1)}}</div><div>{{c1::Phosphofructokinase (PFK) (Step 3)}}</div><div>{{c1::Pyruvate kinase (Step 10)}}</div></div>"<div><img src=""Glycolysis (1).png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=8qij1m7XUhk"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Glycolysis
"<img src=""Glycolysis Hexokinase (3).png""><div><br></div><div>The above reaction is from&nbsp;<u>glycolysis</u></div><div><b><br></b></div><div>The <i style="""">enzyme that catalyzes</i> this reaction is {{c1::hexokinase/glucokinase}}</div>""<div><img src=""Glycolysis Hexokinase Complete.png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=8qij1m7XUhk"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Glycolysis
"<img src=""Glycolysis Phosphoglucose Isomerase.png""><div><br></div><div><div>The above reaction is from&nbsp;<u>glycolysis</u></div></div><div><br></div><div>The <i>enzyme that catalyzes</i> this reaction&nbsp; is {{c1::phosphoglucose isomerase}}<br></div>""<div><img src=""Glycolysis Phosphoglucose Isomerase Complete.png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=8qij1m7XUhk"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Glycolysis
"<img src=""Glycolysis Phosphofructokinase (1).png""><div><br></div><div><div>The above reaction is from&nbsp;<u>glycolysis</u></div></div><div><b><br></b></div><div>The <i>enzyme that catalyzes</i> this reaction {{c1::phosphofructokinase (PFK)}}</div>""<div><img src=""Glycolysis Phosphofructokinase Complete.png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=8qij1m7XUhk"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Glycolysis
"<img src=""Glycolysis Aldolase.png""><div><br></div><div><div>The above reaction is from&nbsp;<u>glycolysis</u></div></div><div><b><br></b></div><div>The <i>enzyme that catalyzes</i> this reaction is {{c1::aldolase}}</div>""<div><img src=""Glycolysis Aldolase Complete.png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=8qij1m7XUhk"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Glycolysis
"<img src=""Glycolysis Aldolase 2.png""><div><br></div><div><div>The above reaction is from&nbsp;<u>glycolysis</u></div></div><div><b><br></b></div><div>The <i>enzyme that catalyzes</i> this reaction is {{c1::aldolase}}</div>""<div><img src=""Glycolysis Aldolase 2 Complete.png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=8qij1m7XUhk"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Glycolysis
"<img src=""Glycolysis Glyceraldehyde 3-Phospate Dehydrogenase.png""><div><br></div><div><div>The above reaction is from&nbsp;<u>glycolysis</u></div></div><div><b><br></b></div><div>The <i>enzyme that catalyzes</i> this reaction is {{c1::glyceraldehyde 3-phosphate dehydrogenase}}</div>""<div><img src=""Glycolysis Glyceraldehyde 3-Phospate Dehydrogenase Complete.png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=8qij1m7XUhk"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Glycolysis
"<img src=""Glycolysis Phosphoglycerate Kinase.png""><div><br></div><div><div>The above reaction is from&nbsp;<u>glycolysis</u></div></div><div><b><br></b></div><div>The <i>enzyme that catalyzes</i> this reaction is {{c1::phosphoglycerate kinase}}</div>""<div><img src=""Glycolysis Phosphoglycerate Kinase Complete.png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=8qij1m7XUhk"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Glycolysis
"<img src=""Glycolysis Phosphoglycerate Mutase.png""><div><br></div><div><div>The above reaction is from&nbsp;<u>glycolysis</u></div></div><div><b><br></b></div><div>The <i>enzyme that catalyzes</i> this reaction is {{c1::phosphoglycerate mutase}}</div>""<div><img src=""Glycolysis Phosphoglycerate Mutase Complete.png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=8qij1m7XUhk"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Glycolysis
"<img src=""Glycolysis Enolase.png""><div><br></div><div><div>The above reaction is from&nbsp;<u>glycolysis</u></div></div><div><b><br></b></div><div>The <i>enzyme that catalyzes</i> this reaction is {{c1::enolase}}</div>""<div><img src=""Glycolysis Enolase Complete.png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=8qij1m7XUhk"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Glycolysis
"<img src=""Glycolysis Pyruvate Kinase (1).png""><div><br></div><div><div>The above reaction is from&nbsp;<u>glycolysis</u></div></div><div><b><br></b></div><div>The <i>enzyme that catalyzes</i> this reaction is {{c1::pyruvate kinase}}</div>""<div><img src=""Glycolysis Pyruvate Kinase Complete.png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=8qij1m7XUhk"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Glycolysis
"<img src=""Glycolysis Triose Phosphate Isomerase.png""><div><br></div><div><div>The above reaction is from&nbsp;<u>glycolysis</u></div></div><div><b><br></b></div><div>The <i>enzyme that catalyzes</i> this reaction is {{c1::triose phosphate isomerase}}</div>""<div><img src=""Glycolysis Triose Phosphate Isomerase Complete.png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=8qij1m7XUhk"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Glycolysis
Glycolysis <u>requires</u> {{c1::2::#}} ATP and <i>produces</i> {{c1::4::#}} ATP"<div><b>A net gain of 2 ATP</b><br></div><div><br></div><div><img src=""Glycolysis Abbreviated.png""></div><div><br><div><img src=""Glycolysis Reactants and Products (1).png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=8qij1m7XUhk"">YouTube Link</a><br></div></div>"MileDown::Biochemistry::Metabolism::Glycolysis
Glycolysis <u>requires</u> {{c1::2::#}} NAD<sup>+</sup>&nbsp;and <i>produces</i> {{c1::2::#}} NADH"<div><div><img src=""Glycolysis Abbreviated.png""><br></div><div><br><div><img src=""Glycolysis Reactants and Products (1).png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=8qij1m7XUhk"">YouTube Link</a></div></div></div><div></div>"MileDown::Biochemistry::Metabolism::Glycolysis
"<img src=""Glycolysis Hexokinase Produces.png""><div><br></div><div><div>The above reaction is from&nbsp;<u>glycolysis</u></div></div><div><b><br></b></div><div>This reaction <u>requires</u> {{c1::ATP}} and&nbsp;<i>produces</i> {{c1::ADP}}</div>""<div><img src=""Glycolysis Hexokinase Complete.png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=8qij1m7XUhk"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Glycolysis
"<img src=""Glycolysis Phosphofructokinase Produces.png""><div><br></div><div><div>The above reaction is from&nbsp;<u>glycolysis</u></div></div><div><b><br></b></div><div>This reaction <u>requires</u> {{c1::ATP}} and&nbsp;<i>produces</i> {{c1::ADP}}</div>""<div><img src=""Glycolysis Phosphofructokinase Complete.png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=8qij1m7XUhk"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Glycolysis
"<img src=""Glycolysis Phosphoglycerate Kinase Produces.png""><div><br></div><div><div>The above reaction is from&nbsp;<u>glycolysis</u></div></div><div><b><br></b></div><div>This reaction <u>requires</u> {{c1::ADP}} and&nbsp;<i>produces</i> {{c1::ATP}}</div>""<div><img src=""Glycolysis Phosphoglycerate Kinase Complete.png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=8qij1m7XUhk"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Glycolysis
"<img src=""Glycolysis Pyruvate Kinase Produces.png""><div><br></div><div><div>The above reaction is from&nbsp;<u>glycolysis</u></div></div><div><b><br></b></div><div>This reaction <u>requires</u> {{c1::ADP}} and&nbsp;<i>produces</i> {{c1::ATP}}</div>""<div><img src=""Glycolysis Pyruvate Kinase Complete.png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=8qij1m7XUhk"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Glycolysis
"<img src=""Glycolysis Glyceraldehyde 3-Phospate Dehydrogenase Produces.png""><div><br></div><div><div>The above reaction is from&nbsp;<u>glycolysis</u></div></div><div><b><br></b></div><div>This reaction <u>requires</u> {{c1::Pi}} and {{c1::NAD<sup>+</sup>}}&nbsp;and it&nbsp;<i>produces</i> {{c1::NADH}}</div>""<div><img src=""Glycolysis Glyceraldehyde 3-Phospate Dehydrogenase Complete.png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=8qij1m7XUhk"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Glycolysis
"<img src=""Glycolysis Enolase Produces.png""><div><br></div><div><div>The above reaction is from&nbsp;<u>glycolysis</u></div></div><div><b><br></b></div><div>This reaction <i>produces</i>&nbsp;{{c1::H<sub>2</sub>O}}</div>""<div><img src=""Glycolysis Enolase Complete.png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=8qij1m7XUhk"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Glycolysis
"<img src=""Gluconeogenesis Pyruvate Carboxylase.png""><div><br></div><div>The above reactions are from <b>gluconeogenesis</b></div><div><br></div><div>The <i>enzymes</i> involved in these two reactions are {{c1::pyruvate carboxylase}}&nbsp;and {{c1::phosphoenolpyruvate carboxykinase (PEPCK)}}</div>""<div><img src=""Gluconeogenesis Pyruvate Carboxylase Complete (1).png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=ydhr0QAyxYg"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Gluconeogenesis
"<img src=""Gluconeogenesis Enolase.png""><div><br></div><div>The above reaction is from&nbsp;<b>gluconeogenesis</b></div><div><b><br></b></div><div>This reaction <u>requires</u>&nbsp;{{c1::H<sub>2</sub>O}}</div>""<div><img src=""Gluconeogenesis Enolase Complete.png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=ydhr0QAyxYg"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Gluconeogenesis
"<img src=""Gluconeogenesis Fructose 1,6-bisphosphatase.png""><div><br></div><div><div>The above reaction is from&nbsp;<b>gluconeogenesis</b></div></div><div><br></div><div>The <i>enzyme that catalyzes</i> this reaction {{c1::fructose 1,6-bisphosphatase}}<br></div>""<div><img src=""Gluconeogenesis Fructose 1,6-bisphosphatase Complete.png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=ydhr0QAyxYg"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Gluconeogenesis
"<img src=""Gluconeogenesis Glucose 6-phosphatase.png""><div><br></div><div><div>The above reaction is from&nbsp;<b>gluconeogenesis</b></div></div><div><b><br></b></div><div>The <u>enzyme that catalyzes</u> this reaction {{c1::glucose 6-phosphatase}}</div>""<div><img src=""Gluconeogenesis Glucose 6-phosphatase Complete.png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=ydhr0QAyxYg"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Gluconeogenesis
The important regulatory enzymes in <b>gluconeogenesis</b> are {{c1::pyruvate carboxylase}}, {{c1::phosphoenolpyruvate (PEP) carboxykinase}}, ,&nbsp; {{c1::fructose 1,6-bisphosphatase}}, and {{c1::glucose 6-phosphatase}}"<div><img src=""Gluconeogenesis (1).png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=ydhr0QAyxYg"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Gluconeogenesis
"<img src=""Gluconeogenesis Pyruvate Carboxylase Activation.png""><div><br></div><div><div>The above reactions are from&nbsp;<b>gluconeogenesis</b></div></div><div><b><br></b></div><div>The conversion of <i>pyruvate to PEP</i> is activated by {{c1::acetyl-CoA}}</div>""<div><img src=""Gluconeogenesis Pyruvate Carboxylase Complete (1).png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=ydhr0QAyxYg"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Gluconeogenesis
In <b>gluconeogenesis</b>, the combination of {{c1::pyruvate carboxylase::enzyme 1}} and {{c1::phosphoenolpyruvate carboxykinase::enzyme 2}} is used to circumvent the&nbsp;action of <i>pyruvate kinase</i>"<div><img src=""Gluconeogenesis Pyruvate Carboxylase Complete (1).png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=ydhr0QAyxYg"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Gluconeogenesis
The {{c1::citric acid cycle}} is a series of reactions that&nbsp;<u>oxidizes</u> <u>acetyl-CoA</u>"<div>It produces G<i>TP</i>, <i>NADH</i>, <i>FADH<sub>2</sub></i>, and <i>CO<sub>2</sub></i><br></div><div><div><br></div><div><img src=""Citric Acid Cycle (2).png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=ubzw64PQPqM"">YouTube Link</a><br></div></div>"MileDown::Biochemistry::Metabolism::Acetyl-CoA MileDown::Biochemistry::Metabolism::Citric_Acid_Cycle
"<img src=""Citrate Synthase.jpg""><div><br></div><div>The above reaction is from the <u>citric acid cycle</u></div><div><br></div><div>The <i>enzyme that catalyzes</i> this reaction is {{c1::citrate synthase}}</div>""<div><img src=""Citrate Synthase Complete.jpg""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=ubzw64PQPqM"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Citric_Acid_Cycle
"<img src=""Acpnitase.jpg""><div><br></div><div>The above reaction is from the&nbsp;<u>citric acid cycle</u></div><div><b><br></b></div><div>Name the <i>enzyme that catalyzes</i> this reaction is {{c1::aconitase}}</div>""<div><img src=""Acpnitase Complete.jpg""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=ubzw64PQPqM"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Citric_Acid_Cycle
"<img src=""Isocitrate Dehydrogenase (1).jpg""><br><div><br></div><div><div>The above reaction is from the <u>citric acid cycle</u></div></div><div><b><br></b></div><div>The <i>enzyme that catalyzes</i> this reaction is {{c1::isocitrate dehydrogenase}}</div>""<div><img src=""Isocitrate Dehydrogenase Complete (1).jpg""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=ubzw64PQPqM"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Citric_Acid_Cycle
"<img src=""Alpha-Ketoglutarate Dehydrogenase Complex.jpg""><br><div><br></div><div><div>The above reaction is from the <u>citric acid cycle</u></div></div><div><b><br></b></div><div>The <i>enzyme that catalyzes</i> this reaction is&nbsp;{{c1::α-ketoglutarate dehydrogenase complex}}</div>""<div><img src=""Alpha-Ketoglutarate Dehydrogenase Complex Complete (1).jpg""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=ubzw64PQPqM"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Citric_Acid_Cycle
"<img src=""Succinyl CoA Synthetase.jpg""><div><br></div><div><div>The above reaction is from the <u>citric acid cycle</u></div></div><div><b><br></b></div><div>The <i>enzyme that catalyzes</i> this reaction is {{c1::succinyl CoA synthetase}}</div>""<div><img src=""Succinyl CoA Synthetase Complete.jpg""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=ubzw64PQPqM"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Citric_Acid_Cycle
"<img src=""Succinate Dehydrogenase.jpg""><div><br></div><div><div>The above reaction is from the <u>citric acid cycle</u></div></div><div><b><br></b></div><div>The <i>enzyme that catalyzes</i> this reaction is {{c1::succinate dehydrogenase}}</div>""<div><img src=""Succinate Dehydrogenase Complete.jpg""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=ubzw64PQPqM"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Citric_Acid_Cycle
"<img src=""Fumarase.jpg""><div><br></div><div><div>The above reaction is from the&nbsp;<u>citric acid cycle</u></div></div><div><b><br></b></div><div>The <i>enzyme that catalyzes</i> this reaction is {{c1::fumarase}}</div>""<div><img src=""Fumarase Complete.jpg""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=ubzw64PQPqM"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Citric_Acid_Cycle
"<img src=""Malate Dehydrogenase.jpg""><div><br></div><div><div>The above reaction is from the&nbsp;<u>citric acid cycle</u></div></div><div><b><br></b></div><div>The <i>enzyme that catalyzes</i> this reaction is {{c1::malate dehydrogenase}}</div>""<div><img src=""Malate Dehydrogenase Complete.jpg""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=ubzw64PQPqM"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Citric_Acid_Cycle
"<img src=""Citrate Synthase Reactants.jpg""><div><br></div><div><div>The above reaction is from the&nbsp;<u>citric acid cycle</u></div></div><div><b><br></b></div><div>This reaction <u>requires</u> {{c1::oxaloacetate}} and {{c1::acetyl-CoA}} and <i style="""">produces</i> {{c1::citrate}} and {{c1::CoA}}</div>""<div><img src=""Citrate Synthase Complete.jpg""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=ubzw64PQPqM"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Citric_Acid_Cycle
"<img src=""Isocitrate Dehydrogenase Reactants.jpg""><div><br></div><div><div>The above reaction is from the <u>citric acid cycle</u></div></div><div><br></div><div>This reaction <u>requires</u> {{c1::isocitrate}} and {{c1::NAD<sup>+</sup>}}&nbsp;and <i>produces</i> {{c1::α-ketoglutarate}}, {{c1::NADH}}, and {{c1::CO<sub>2</sub>}}</div>""<div><img src=""Isocitrate Dehydrogenase Complete (1).jpg""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=ubzw64PQPqM"">YouTube Link</a></div>"MileDown::Biochemistry::Metabolism::Citric_Acid_Cycle
"<img src=""Alpha-Ketoglutarate Dehydrogenase Complex Reactants.jpg""><div><br></div><div><div>The above reaction is from the <u>citric acid cycle</u></div></div><div><b><br></b></div><div>This reaction <u>requires</u>&nbsp;{{c1::α-ketoglutarate}}, {{c1::NAD<sup>+</sup>}}, and&nbsp;{{c1::CoA}} and <i>produces</i> {{c1::succinyl CoA,}} {{c1::NADH}}, and {{c1::CO<sub>2</sub>}}</div>""<div><img src=""Alpha-Ketoglutarate Dehydrogenase Complex Complete (1).jpg""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=ubzw64PQPqM"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Citric_Acid_Cycle
"<img src=""Succinyl CoA Synthetase Reactants.jpg""><div><br></div><div><div>The above reaction is from the <u>citric acid cycle</u></div></div><div><b><br></b></div><div>This reaction <u>requires</u>&nbsp;{{c1::succinyl CoA}}, {{c1::GDP}}, and {{c1::Pi}} and <i>produces</i>&nbsp;{{c1::succinate}}, {{c1::GTP}}, and {{c1::CoA}}</div>""<div><img src=""Succinyl CoA Synthetase Complete.jpg""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=ubzw64PQPqM"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Citric_Acid_Cycle
"<img src=""Fumarase Reactants.jpg""><div><br></div><div><div>The above reaction is from the <u>citric acid cycle</u></div></div><div><b><br></b></div><div>This reaction <u>requires</u>&nbsp;{{c1::H<sub>2</sub>O}}</div>""<div><img src=""Fumarase Complete.jpg""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=ubzw64PQPqM"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Citric_Acid_Cycle
"<img src=""Malate Dehydrogenase Reactants.jpg""><div><br></div><div><div>The above reaction is from the <u>citric acid cycle</u></div></div><div><b><br></b></div><div>This reaction <u>requires</u> {{c1::malate}} and {{c1::NAD<sup>+</sup>}}&nbsp;and <i>produces</i> {{c1::oxaloacetate}}, {{c1::NADH}}, and {{c1::H<sup>+</sup>}}</div>""<div><img src=""Malate Dehydrogenase Complete.jpg""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=ubzw64PQPqM"">YouTube Link</a></div>"MileDown::Biochemistry::Metabolism::Citric_Acid_Cycle
The three <b>regulatory enzymes</b> in the <u>citric acid cycle</u>&nbsp;are:<div><br></div><div>{{c1::Citrate synthase}}<div>{{c1::Isocitrate dehydrogenase}}</div><div>{{c1::α-ketoglutarate dehydrogenase complex}}</div></div>"<div><img src=""Citric Acid Cycle Regulatory Steps.png""></div><div><br></div><div><img src=""Citric Acid Cycle Regulatory Enzymes (2).png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=ubzw64PQPqM"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Citric_Acid_Cycle
The&nbsp;<i>rate limiting enzyme</i> in the <u>citric acid cycle</u>&nbsp;is {{c1::isocitrate dehydrogenase}}"<div><img src=""Citric Acid Cycle Regulatory Steps.png""></div><div><br></div><div><div><img src=""Citric Acid Cycle Regulatory Enzymes (2).png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=ubzw64PQPqM"">YouTube Link</a></div></div>"MileDown::Biochemistry::Metabolism::Citric_Acid_Cycle
The <u>citric acid cycle</u> requires {{c1::3::#}} <b>NAD<sup>+</sup></b> and produces {{c1::3::#}} <u>NADH</u>"<div><img src=""Citric Acid Cycle Reactants and Products (1).png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=ubzw64PQPqM"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Citric_Acid_Cycle
The <u>citric acid cycle</u> requires {{c1::1::#}} <i>FAD</i> and produces {{c1::1::#}} <b>FADH<sub>2</sub></b>"<div><br></div><div><img src=""Citric Acid Cycle Reactants and Products (1).png""><br></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=ubzw64PQPqM"">YouTube Link</a></div>"MileDown::Biochemistry::Metabolism::Citric_Acid_Cycle
The <u>citric acid cycle</u> requires {{c1::1::#}} <b>GDP</b> and produce {{c1::1::#}} <i>GTP</i>"<div><br></div><div><img src=""Citric Acid Cycle Reactants and Products (1).png""><br></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=ubzw64PQPqM"">YouTube Link</a></div><div></div>"MileDown::Biochemistry::Metabolism::Citric_Acid_Cycle
The <u>citric acid cycle</u> sends electrons to the <i>electron transport chain</i> within the electron carriers&nbsp;{{c1::NADH}} and {{c1::FADH<sub>2</sub>}}"<div><img src=""Oxidative Phosphorylation.png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=C8VHyezOJD4"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Citric_Acid_Cycle
<u>Complex II&nbsp;</u>in the ETC is part of the {{c1::citric acid cycle}}"<div><img src=""Succinate Dehydrogenase Complete.jpg""></div><div><br></div><div><div><img src=""Oxidative Phosphorylation (1).png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=ay9WIAkoa1Y"">YouTube Link</a></div></div>"MileDown::Biochemistry::Metabolism::ETC
"<div><img src=""Pentose Phosphate Pathway Ribose 5-Phosphate (2).png""></div><div><br></div><div>The <b>pentose phosphate pathway</b> produces {{c1::ribose 5-phosphate}} and sends for use in <u>nucleotide synthesis</u><br></div>""<div><br></div><div>Ribose 5 phosphate is the <i>key product</i></div><div><img src=""Pentose Phosphate Pathway (2).png""></div><div><br></div><div><a href=""https://www.khanacademy.org/test-prep/mcat/biomolecules/carbohydrate-metabolism/v/pentose-phosphate-pathway"">Khan Academy Link</a><br></div>"MileDown::Biochemistry::Metabolism::Pentose_Phosphate_Pathway
The <i>urea cycle</i> connects to the <u>citric acid cycle</u> using the compounds {{c1::oxaloacetate}} and {{c1::fumarate}}"<div><img src=""Urea Cycle.png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=K3rVr_SfXo8"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Urea_Cycle
<u>Hexokinase</u> is inhibited by {{c1::glucose 6-phosphate}}"<div><br></div><div>Negative feedback</div><div><br></div><div><img src=""Hexokinase Regulation.png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=OG4A3Fkitvw"">YouTube Link</a></div>"MileDown::Biochemistry::Metabolism::Glycolysis
{{c1::Phosphofructokinase}} is the <i>enzyme that catalyzes the committed step</i> of <u>glycolysis</u>"<div>After this step, the sugar molecule is <b>committed to completing Glycolysis</b>&nbsp;</div><div><br></div><div>Prior to this step, the sugar molecule could have been <u>redirected to be converted to glycogen</u></div><div><br></div><div><img src=""Glycolysis (1).png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=QEIWcOY0x0g"">YouTube Link</a></div>"MileDown::Biochemistry::Metabolism::Glycolysis
<i>Phosphofructokinase</i> is <u>inhibited</u> by {{c1::ATP}}, {{c1::citrate}}, and {{c1::H+}}"<div><img src=""Phosphofructokinase Regulation.png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=OG4A3Fkitvw"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Glycolysis
<i>Phosphofructokinase</i> is <b>activated</b> by {{c1::AMP}} and {{c1::fructose 2,6-bisphosphate}}"<div><img src=""Phosphofructokinase Regulation.png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=OG4A3Fkitvw"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Glycolysis
<b>Pyruvate kinase</b> is <i>activated</i> by {{c1::fructose 1,6-bisphosphate}}"<div><img src=""Pyruvate Kinase Regulation.png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=OG4A3Fkitvw"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Glycolysis
{{c1::Glycogenesis}} is the <i>production of&nbsp;glycogen</i>&nbsp;from sugar"<div>Occurs in&nbsp;the <b>liver</b> and <b>muscles</b></div><div><b><br></b></div><div><font color=""#195ab3""><img src=""Glycogenesis (4).png""></font></div><div><font color=""#195ab3""><br></font></div><div><a href=""https://www.youtube.com/watch?v=3FHKw2aS_Z0"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Glycogen
The <u>glycolysis intermediate</u> {{c1::glucose 6-phosphate}} feeds into <i>glycogenesis</i>"<div><img src=""Glycogenesis (4).png"" style=""color: rgb(25, 90, 179);""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=3FHKw2aS_Z0"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Glycogen MileDown::Biochemistry::Metabolism::Glycolysis
<b>Gluconeogenesis</b> takes place in the {{c1::liver::organ}} and {{c1::kidneys::organ}}<div><br></div><div>90% of glucose from liver</div><div>10% from kidney</div><div>40% from kidney after prolonged fasting</div>MileDown::Biochemistry::Metabolism::Gluconeogenesis
The glycolysis enzyme <i>pyruvate kinase is irreversible</i>. This is why in <b>gluconeogenesis</b>,&nbsp;pyruvate must first be converted to {{c1::oxaloacetate}} before becoming phosphoenolpyruvate"<div><img src=""Gluconeogenesis Pyruvate Carboxylase Complete (1).png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=ydhr0QAyxYg"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Gluconeogenesis
The <i>rate limiting enzyme</i> of the <b>pentose phosphate pathway</b> is {{c1::glucose 6-phosphate dehydrogenase}}"<div>This step creates&nbsp;<u>NADPH</u><br></div><div><br></div><div><img src=""Pentose Phosphate Pathway Oxidative Stage.png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=nMWmmJLEI9I"">YouTube Link</a></div>"MileDown::Biochemistry::Metabolism::Pentose_Phosphate_Pathway
The <b>pentose phosphate pathway</b> occurs in the {{c1::cytosol::part of cell}}"<div><img src=""HMP Shunt Location.jpg""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=nkTDi2WIm4w"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Pentose_Phosphate_Pathway
"<img src=""Reaction Pathway Locations Blank.png""><div><br></div><div><b>Glycolysis, pyruvate oxidation, glycogenolysis, and fatty acid synthesis</b> all occur in the {{c1::cytoplasm::part of cell}}</div><div><br></div><div><u>The citric acid cycle, oxidative phosphorylation, and beta oxidation</u> all occur in the {{c1::mitochondria::part of cell}}</div>""<div><img src=""Reaction Pathway Sites.png""><br></div>"MileDown::Biochemistry::Metabolism MileDown::Biochemistry::Metabolism::Citric_Acid_Cycle MileDown::Biochemistry::Metabolism::ETC MileDown::Biochemistry::Metabolism::Fatty_Acids MileDown::Biochemistry::Metabolism::Glycogen MileDown::Biochemistry::Metabolism::Glycolysis
The <u>citric acid cycle</u> produces {{c1::GTP}}, {{c1::NADH}}, {{c1::FADH<sub>2</sub>}}, and {{c1::CO<sub>2</sub>}}"<div><img src=""Citric Acid Cycle (2).png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=ubzw64PQPqM"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Citric_Acid_Cycle
<div><i>Isocitrate dehydrogenase</i>, the rate limiting enzyme of the citric acid cycle is <b>activated</b> by {{c1::ADP}} or&nbsp;{{c1::NAD<sup>+</sup>}}</div>"<div><img src=""Citric Acid Cycle Regulatory Enzymes (2).png""><br></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=ubzw64PQPqM"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Citric_Acid_Cycle
<i>Isocitrate dehydrogenase</i>, the rate limiting enzyme of the citric acid cycle is <u>inhibited</u> by {{c1::ATP}} or&nbsp;{{c1::NADH}}"<div><img src=""Citric Acid Cycle Regulatory Enzymes (2).png""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=ubzw64PQPqM"">YouTube Link</a></div><div></div>"MileDown::Biochemistry::Metabolism::Citric_Acid_Cycle
The <i>citric acid cycle</i> occurs in the {{c1::mitochondrial matrix}}"<div><br></div><div><img src=""Eukaryotes CAC Location.jpg"" style=""color: rgb(25, 90, 179);""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=ubzw64PQPqM"">YouTube Link</a><br></div>"MileDown::Biochemistry::Metabolism::Citric_Acid_Cycle
<u>Myoglobin</u> contains {{c1::one::#}} heme group"<div><img src=""Myoglobin.jpg""></div><div><br></div><div><a href=""https://www.youtube.com/watch?v=XUI5vGfNYZY"">YouTube Link</a><br></div>"MileDown::Biology::Cardiovascular_System
"Water's {{c1::polarity}} and {{c1::H-bonding}} account for its unique properties such as <b>high boiling point (100°C), high freezing point (0°C), high heat capacity, and high cohesiveness</b>"Water helps maintain gradient in blood due to polarity (specifically the negative O)<br>Allows water to act as acid and base
Stomach pH before digestion is {{c1::4}} and during digestion is {{c1::2}}
{{c1::Phosphate}} is the major <i>intracellular</i> buffer while {{c1::bicarbonate}} is the major <b>extracellular</b> buffer
{{c1::Acidosis}} occurs when <i>hypoventilating</i>, which is the retainment or accumulation of CO2
{{c1::Alkalosis}} occurs when <b>hyperventilating</b> or vomiting, which eliminates CO2
What is the normal pH range in acid-base disturbance problems?pH 7.35 to 7.45
Acidoses occurs when pH is below {{c1::7.35}}, alkalosis occurs when pH is above {{c1::7.45}}.
Which is true about water?<br>a. The bond angle between hydrogens is less than 100 degrees<br>b. The low boiling point is partly explained by the dipolar character<br>c. Ionic bonding accounts for water’s highly cohesive nature<br>d. Water only serves as a base in the renal system<br>e. Exhibits a partial negative charge on the oxygen atomE
Nate had some steak two hours ago and is currently digesting. He also took some aspirin to relieve post-workout muscle aches. Which statement is true?<br><br>a. Aspirin is in a protonated state since stomach pH &lt; pKa and will readily be absorbed into the bloodstream<br>b. Aspirin is in a deprotonated state since stomach pH &lt; pKa and will readily be absorbed into the bloodstream<br>c. Aspirin is in a protonated state since stomach pH &gt; pKA and will readily be absorbed into the bloodstream<br>d. Aspirin is in a deprotonated state since stomach pH &gt; pKa and will readily be absorbed into the bloodstream<br>e. Aspirin is in a zwitterion state due to ionic interference<i>A</i><br>Aspirin has a pKa of 3.5, stomach pH during digestion is 2<br>pH &lt; pKa, which means Aspirin will be protonated<br>When aspirin is protonated, it is readily absorbed into the blood
Glucose and galactose are {{c1::C4 epimers}} to each other"<img src=""paste-417fef39d926c5fb091f066ab37c23bbbfba5793.jpg"">"
In diabetic cataractogenesis, {{c1::sorbitol dehydrogenase}} stops working, leading to elevated levels of {{c1::sorbitol}}"<img src=""paste-104fd20694ec9b536773180375ac2628c3579cd3.jpg"">"
Na+/K+ ATPase is a <i>primary active transport</i> because it requires energy {{c1::directly from ATP}}
{{c1::Extrinsic apoptotic}} pathway is when signaling on cell membrane activates <i>caspases, apoptosomes, and nucleases</i>
{{c1::Intrinsic apoptotic}} pathway is the {{c2::<i>loss of mitochondrial cytochrome C</i>}} which activates apoptosomesA signal is sent to mitochondria, which then loses cytochrome C and signal apoptosomes
In nature, most of the amino acids found in living organisms are of the {{c1::L}}-configuration due to <i>enzymatic processes</i>, as they are the only amino acids incorporated into proteins
{{c1::Glycine}} is the only non-chiral amino acid
Glycine is an important precursor for {{c1::hemes}} and {{c1::purines}}
At physiological pH 7.4, the amine group of an amino acid is {{c1::(+)}} charged while the carboxylic group is {{c1::(-)}} charged
{{c1::Nonpolar}} side chains are important for <b>protein folding</b> due to their <b>hydrophobicity</b>
A {{c1::zwitterion}} is an electrically <b>neutral</b> amino acidAmino group is +<br>Carboxyl group is -<br>Net charge = 0 (PI point)
pKa indicates acidic strength. The lower the pKa value, the {{c1::stronger}} the acid
pH {{c1::&gt;}} pKa = release of a proton to become anionic
pH {{c1::&lt;}} pKa = adoption of a proton to become cationic
pH {{c1::=}} pKa = electrically neutral zwitterion
The two semi-essential amino acids are {{c1::histidine and arginine}}
Children make <i>histidine</i> at a low rate, so they need it in diet to maintain a {{c1::nitrogen balance}}
Children may not have enough {{c1::arginine}} due to it being converted to <u>ornithine in the urea cycle</u>. Therefore, they need to obtain it through diet.Adults generate enough arginine through the urea cycle but children do not, so arginine is essential in children but not adults
{{c1::Covalent disulfide bonds}} that occur between two adjacent <b>cysteine sulfhydryls</b> are important for {{c1::stabilizing the structure of proteins}}&nbsp;Due to the high reactivity of the R group
What is <i>histidine</i> a precursor of and why is the resulting product important?Precursor of histamine, which is important for inflammatory responses and acting as a neurotransmitter
{{c1::Arginine::amino acid}} and {{c1::lysine::amino acid}} are abundantly found in <i>histones</i>, which associate with DNA to make chromosomes
{{c1::Glutamate}} is a major <i>excitatory</i> neurotransmitter
Describe the primary structure of a protein and the configuration their R groups are arranged inLinear chain of amino acids in a peptide or protein in which the R groups are arranged in <i>trans-configuration</i> to adopt the <u>lowest energy configuration</u> (minimize steric hindrance)
Describe the secondary structure of a protein&nbsp;Local folded structure due to interactions of the polypeptide backbone into alpha helices (four residue turns) and beta strands
Secondary protein structure is stabilized by {{c1::Intramolecular}} and sometimes {{c1::intermolecular hydrogen bonding}}
Describe the tertiary structure of a proteinSpatial arrangement of the secondary structure elements resulting in formation of protein structure/fold
Tertiary structure is held together by {{c1::non-covalent}} interactions, {{c1::disulfide}} bonds, and {{c1::metal ion coordination}}"<img src=""paste-5037a82283a9ac040b3867ff824e1e72d21cc425.jpg"">"
pH of arterial blood plasma is {{c1::7.4}}
pH of the inner mitochondrial matrix is {{c1::7.5}}
"When pH &lt; {{c1::3.5::numerical value}}, aspirin's side chain is {{c1::protonated}} and aspirin gets absorbed"Aspirin has a side carboxyl group with a pKa of 3.5
Lysosomes have a pH of {{c1::5.5}}
Henderson-Hasselbalch equation:&nbsp;"<img src=""paste-864f6c6b0f34c017d1d2cce944bfbc290dacc5d7.jpg"">"
Most buffers work best when the pH scale of pKa is {{c1::+/- 1}}
Amino acids are <i>zwitterions</i> at physiological pH, so buffering capacity is dependent on {{c1::their side groups}}
The {{c1::phosphate}} buffer is the major <b>intracellular</b> buffer system with a pH range of {{c1::6.4 to 7.4}}"<img src=""paste-d2237951efd7e310e0a31fa6424cc8fb9936c1b8.jpg"">"
The {{c1::bicarbonate}} buffer system is the major <b>extracellular</b> buffer system with a pH range of {{c1::7.36 to 7.44}}"Main buffer system of blood plasma<br><img src=""paste-a9af1d170b7136354f82943f976ac8d3aca2f458.jpg"">"
In the bicarbonate buffer system, {{c1::carbonic anhydrase::enzyme}} is responsible for catalyzing the reaction between <b>CO2 and H2O</b> to produce bicarbonate (H2CO3)"<img src=""paste-35290bf4f9e09e6709eed1ac8ed203db3b20479e.jpg"">"
{{c1::Alkalosis}} occurs when the kidney is malfunctioningKidney malfunction leads to retainment of bicarbonate (HCO3-), which is <i>basic</i><br>Retainment of bicarbonate increases the blood pH, which leads to alkalosis
{{c1::Acidosis}} occurs when diarrhea occursDiarrhea eliminates bicarbonate (HCO3-) through the digestive system<br>Bicarbonate is basic, so removing bicarbonate will lower blood pH and lead to acidosis
{{c1::Respiratory acidosis}} is when <u>hypoventilation or pulmonary obstruction</u> leads to the accumulation of CO2Accumulation of CO2 (acidic) increases [H+], which lowers blood pH
{{c1::Respiratory alkalosis}} is when <i>hyperventilation</i> leads to elimination of CO2Elimination of CO2 (acidic) leads to decrease in [H+] in the blood, which increases pH
Altitude causes {{c1::respiratory alkalosis}}, which can be treated by <u>acetazolamide</u>"Acetazolamide blocks carbonic anhydrase in order to decrease the blood pH<br><br><img src=""paste-35290bf4f9e09e6709eed1ac8ed203db3b20479e.jpg"">"
{{c1::Acetazolamide}} can treat <b>altitude sickness</b> ({{c1::respiratory alkalosis}}) by blocking {{c2::carbonic anhydrase}} to make the blood more acidic"<img src=""paste-35290bf4f9e09e6709eed1ac8ed203db3b20479e.jpg"">"
{{c1::Metabolic acidosis}} can be caused by <i>diarrhea or increased acid production</i>Diarrhea is loss of base (decreaes pH)<br>Increased acid production can be caused by <u>lactic acid build up, DKA, or defect in odd chain FA metabolism</u>
{{c1::Metabolic alkalosis}} can be caused by <u>ingestion of too much base (TUMS) or vomiting</u>Vomiting is loss of acid (increases pH)
{{c1::Hyperammonemia}} is <i>alkalosis</i> caused by an enzyme defect in the <u>urea cycle</u> that leads to increased {{c1::ammonia}} levels<br>Ammonia picks up H+ in the blood (decreases blood [H+]) and forms ammonium (NH4+)
Normal pH range in acid-base disturbances is {{c1::7.35 to 7.45}}
Normal metabolic component (HCO3-) levels in acid-base disturbances range from {{c1::22 to 28}}
Normal respiratory component (PaCO2) levels in acid-base disturbances range from {{c1::32 to 48}}
Eric is preparing for his Biochemistry medical school exam and begins to hyperventilate. Respiratory Rate = 36 bpm, Heart rate = 124 bpm, BP = 124/82 right arm sitting. ABG shows pH = 7.55 CO2 = 18 HCO3 = 24. Which is suspected based on the labs provided?<br><br>a. Metabolic acidosis without compensation<br>b. Metabolic alkalosis with compensation<br>c. Respiratory acidosis with compensation<br>d. Respiratory acidosis without compensation<br>e. Respiratory alkalosis without compensation<i>E</i><br>Hyperventilation hints at respiratory alkalosis<br>pH &gt; normal range of <b>7.35 to 7.45</b> indicating alkalosis<br>The respiratory component (CO2) is below the normal range of <b>32 to 48</b> (due to hyperventilation blowing off a lot of CO2), indicating a respiratory alkalosis<br>The metabolic component (HCO3-) is within normal range of <b>22 to 28</b>, indicating that there is no metabolic compensation
{{c1::Altitude sickness}} is the major cause of respiratory alkalosisAltitude can cause hyperventilation (respiratory alkalosis)
Glucose + fructose = {{c1::sucrose}} =&nbsp;{{c1::É‘-D-glucose(1,2)-É‘-fructose}}
Glucose + galactose = {{c1::lactose}} = {{c1::β-D-galactose(1,4)-glucose}}
Glucose + glucose = {{c1::maltose}} = {{c1::É‘-D-glucose (1,4)-glucose}}
The {{c1::R groups}} of amino acids are responsible for their polarity
{{c1::Aldoses}} have a C=O on C1, while {{c1::ketoses}} have a C=O on C2<br>Aldoses end in <i>-ose</i>, and have a terminal aldehyde group<br>Ketoses end in <u>-ulose</u>, and have a terminal ketone group
Glucose and galactose only differ at {{c1::C-4}}"<img src=""paste-5dfefeddd379cf60f43bced41137476b226ccae7.jpg"">"
Glucose and mannose only differ at {{c1::C-2}}"<img src=""paste-761bf3aca7d357092a83ca37384adb761ebbc0b9.jpg"">"
Glucose and fructose are {{c1::structural isomers}}, while glucose and galactose are {{c1::stereoisomers}}"<img src=""paste-2ae2f3fe4aa897e3f96157e6c2b8d319debc1387.jpg""><img src=""paste-909ebe6ffcd3515f5d50567a532840151a455bce.jpg""><img src=""paste-1dc688a375b8ecce80a351dbf2d1e3ee81214ff3.jpg"">"
7c580963d7ea4420a81350e37868a407-ao-1"<img src=""paste-884c9cde3a6e64536da03633d7d4b40b4c463470.jpg"" />""<img src=""7c580963d7ea4420a81350e37868a407-ao-1-Q.svg"" />""<img src=""7c580963d7ea4420a81350e37868a407-ao-1-A.svg"" />""<img src=""7c580963d7ea4420a81350e37868a407-ao-O.svg"" />"
7c580963d7ea4420a81350e37868a407-ao-2"<img src=""paste-884c9cde3a6e64536da03633d7d4b40b4c463470.jpg"" />""<img src=""7c580963d7ea4420a81350e37868a407-ao-2-Q.svg"" />""<img src=""7c580963d7ea4420a81350e37868a407-ao-2-A.svg"" />""<img src=""7c580963d7ea4420a81350e37868a407-ao-O.svg"" />"
7c580963d7ea4420a81350e37868a407-ao-3"<img src=""paste-884c9cde3a6e64536da03633d7d4b40b4c463470.jpg"" />""<img src=""7c580963d7ea4420a81350e37868a407-ao-3-Q.svg"" />""<img src=""7c580963d7ea4420a81350e37868a407-ao-3-A.svg"" />""<img src=""7c580963d7ea4420a81350e37868a407-ao-O.svg"" />"
03872683c8d4480cac616527544dacf1-ao-1"<img src=""paste-fbdce976349066260bd5d2f7e60244bc1b950946.jpg"">""<img src=""03872683c8d4480cac616527544dacf1-ao-1-Q.svg"" />""<img src=""03872683c8d4480cac616527544dacf1-ao-1-A.svg"" />""<img src=""03872683c8d4480cac616527544dacf1-ao-O.svg"">"
03872683c8d4480cac616527544dacf1-ao-2"<img src=""paste-fbdce976349066260bd5d2f7e60244bc1b950946.jpg"" />""<img src=""03872683c8d4480cac616527544dacf1-ao-2-Q.svg"" />""<img src=""03872683c8d4480cac616527544dacf1-ao-2-A.svg"" />""<img src=""03872683c8d4480cac616527544dacf1-ao-O.svg"" />"
03872683c8d4480cac616527544dacf1-ao-3"<img src=""paste-fbdce976349066260bd5d2f7e60244bc1b950946.jpg"" />""<img src=""03872683c8d4480cac616527544dacf1-ao-3-Q.svg"" />""<img src=""03872683c8d4480cac616527544dacf1-ao-3-A.svg"" />""<img src=""03872683c8d4480cac616527544dacf1-ao-O.svg"" />"
d6e64b4b78954ab2a24d926cf2aedd8a-ao-1"<img src=""paste-fbdce976349066260bd5d2f7e60244bc1b950946.jpg"" />""<img src=""d6e64b4b78954ab2a24d926cf2aedd8a-ao-1-Q.svg"" />""<img src=""d6e64b4b78954ab2a24d926cf2aedd8a-ao-1-A.svg"" />""<img src=""d6e64b4b78954ab2a24d926cf2aedd8a-ao-O.svg"" />"
d6e64b4b78954ab2a24d926cf2aedd8a-ao-2"<img src=""paste-fbdce976349066260bd5d2f7e60244bc1b950946.jpg"" />""<img src=""d6e64b4b78954ab2a24d926cf2aedd8a-ao-2-Q.svg"" />""<img src=""d6e64b4b78954ab2a24d926cf2aedd8a-ao-2-A.svg"" />""<img src=""d6e64b4b78954ab2a24d926cf2aedd8a-ao-O.svg"" />"
d6e64b4b78954ab2a24d926cf2aedd8a-ao-3"<img src=""paste-fbdce976349066260bd5d2f7e60244bc1b950946.jpg"" />""<img src=""d6e64b4b78954ab2a24d926cf2aedd8a-ao-3-Q.svg"" />""<img src=""d6e64b4b78954ab2a24d926cf2aedd8a-ao-3-A.svg"" />""<img src=""d6e64b4b78954ab2a24d926cf2aedd8a-ao-O.svg"" />"
alcohol + aldehyde = {{c1::hemiacetal::cyclization structure}}"<img src=""paste-d62aad06f7ad32f355e9244a5dcf394f7cb26c4e.jpg""><br><img src=""paste-fecc2a41c2fa0a31770859d330e9b34c923fb2e1.jpg"">"
alcohol + ketone = {{c1::hemiketal::cylcization structure}}"<img src=""paste-6762183e6b6897d4cb27269188fb958fe777a74c.jpg""><br><img src=""paste-da9a4981df1beea2499a5a4b371eec6d73493f7d.jpg"">"
Ring closure results in {{c1::alpha configuration}} if the -OH points down and {{c1::beta configuration}} if the -OH points points up"<img src=""paste-1f1635908cec284831c379f32373c0ed3ed81280.jpg""><br><img src=""paste-5bc393925c29404443da333d1ff4b843dfcc611b.jpg""><br>"
In ring closure, {{c1::beta}} configuration is more stable due to having <u>lower steric hindrance</u>
{{c1::Pyranose}} is the most stable ring configuration&nbsp;"Pyranose are saccharides that have a 6 membered ring with 5 carbons and 1 oxygen<br><img src=""paste-7daa92787eed40be52f5f2a3dabf8a218174114e.jpg"">"
Ribose is always in the {{c1::beta}} configuration&nbsp;"<img src=""paste-22e0e3ccf8a1b615eae986259b4fe6e891d0881f.jpg""><br>Phosphate connects to C5<br>Base connects to C1"
A <b>nitrogenous base</b> connects to the {{c1::C1::carbon number}} of ribose, and a <i>phosphate</i> connects to the {{c1::C5::carbon number}} of ribose"<img src=""paste-22e0e3ccf8a1b615eae986259b4fe6e891d0881f.jpg""><br><img src=""paste-3a1f55e27810fa0e093532d7cfb3536fb02f3e93.jpg"">"
<b>Glycosidic bonds</b> are formed by {{c1::condensation}} reactions"Results in loss of a water molecule<br><img src=""paste-90761f538143af03c3367a9b17474ebece0ab7e1.jpg"">"
{{c2::Lactose intolerance}} is when patients lack the {{c1::lactase}} enzyme and the patient presents with <i>diarrhea, bloating, abdominal pain, and flatulence</i>"Lactase cleaves the β-D-galactose(1,4)-glucose bond of lactose<br><img src=""paste-02e34e377a2e135c72a33b665d397ddba3ccc043.jpg"">"
{{c1::Mucopolysaccharides (Glycosaminoglycans, GAGS)}} occur mainly in the <u>extracellular matrix</u> and <u>form biofilms</u> that accumulate at interphases (i.e. teeth)"<br>Long, unbranched, and consist of repeating disaccharide monomers<br><img src=""paste-99a81428740ac26b272d3fd780ea007214241e6b.jpg"">"
{{c1::Hyaluronic acid}} is a glycosaminoglycan (GAG) that is an important component of <b>synovial fluid</b>
{{c1::Dermatan sulfate}} is a glycosaminoglycan (GAG) found mostly in <i>skin</i>
{{c1::Chondroitin sulfate}} is a glycosaminoglycan (GAG) found mostly in <i>cartilage</i>
{{c1::Heparan sulfate}} is a glycosaminoglycan (GAG) that is a <b>proteoglycan</b> found in all animal tissue
{{c1::Keratan sulfate}} is a glycosaminoglycan (GAG)&nbsp;involved in <i>scar repair and signaling in cornea</i>
{{c1::Proteoglycans}} are GAGs that are <i>covalently</i> bound to protein<br>Act as <b>lubricants and shock absorbers</b> due to water retention, volume, and strength<br>Organize saccharide chains
{{c1::Proteoglycans}} act as <b>lubricants and shock absorbers</b> due to water retention, volume, and strength
{{c1::Glycoproteins}} are saccharides bound to proteins via <u>glycosylation</u><br><i>Almost all blood cells are glycosylated</i>
{{c1::Hurler syndrome}} is an <i>autosomal recessive</i>&nbsp;lysosomal storage disease&nbsp;caused by {{c1::alpha-L-iduronidase}} deficiency<br>Build up of <u>heparan sulfate</u> and <u>dermatan sulfate</u>
Symptoms of {{c1::Hurler Syndrome}} include coarsening of facial features (gargoylism) and <b>corneal clouding</b>"<img src=""paste-bbda5d15539a0b4bde5c2d5be5ed0b31fa456f8b.jpg"">"
{{c1::Hunter Syndrome}} is an {{c2::<i>X-linked recessive</i>}} lysosomal storage disease&nbsp;caused by {{c1::<i>iduronate-2-sulfatase</i>}} deficiency&nbsp;Progressive chronic disease
Symptoms of {{c1::Hunter Syndrome}} include <u>skeletal changes, stiff joints, behavioral problems, hyperactivity, and aggression</u>"<img src=""paste-cd354104b86169bd32602ce70f9d50399a9af148.jpg"">"
Diabetes is a major cause of blindness.<br>Mechanism:<br>Elevated intracellular {{c1::glucose}} levels activate {{c1::aldose reductase}}, which <i>reduces</i> {{c1::glucose}} to {{c1::sorbitol}}. While elevated {{c1::sorbitol}} levels would normally activate {{c1::sorbitol dehydrogenase}}, this enzyme is dysfunctional in patients with {{c1::diabetic cataractogenesis}}. This leads to accumulation of {{c1::sorbitol}} which causes <b>osmotic damage</b> as fluid accumulates. This leads to glycation of proteins and formation of {{c1::cataracts}}"<img src=""paste-b545f50836b9e6b93613cf8defd4976f8dbed083.jpg"">"
"Which is true regarding the structure shown?<br>a. L-isomer is naturally occurring <br>b. Makes up the core component of cell membranes <br>c. Structural isomer of galactose <br>d. Considered an aldose <br>e. Forms nucleotides<br><img src=""paste-d2b9f9dd08ad623eb0e23651ffa73fd441ae2379.jpg"">"<i>D</i><br>Has a terminal aldehyde group (H-C=O)
A 45 year old patient with a history of diabetes presents with concerns of worsening vision. If aldose reductase is malfunctioning in this patient, levels of what would be expected to increase?<br><br>a. glucose <br>b. sorbitol <br>c. fructose <br>d. galactose <br>e. lactose"<i>A</i><br><img src=""paste-653eabc92b178b8f4e46c902db1646d841b4fbf1.jpg"">"
Fatty acids have a {{c1::polar carboxylic}} head and a {{c1::nonpolar hydrocarbon}} tail"<img src=""paste-9279f08e1a258723dd1e25225acd1e9547c9ca3f.jpg"">"
Saturated fatty acids consist of {{c1::only single}} bonds while unsaturated fatty acids consist of {{c1::one or more double bonds}}. This is why saturated fatty acids tend to be {{c1::solid}} at room temperature while unsaturated fatty acids tend to be {{c1::liquid}} at room temperature.
{{c1::Cis}}-fatty acids occur naturally while {{c1::trans}}-fatty acids only form by synthetic processes (disease)"<img src=""paste-197ca516e95e6750e7b14406b642f5d64393d79e.jpg"">"
When numbering fatty acids, {{c1::Omega}} starts at the methyl end while {{c1::Delta}} starts at the carboxyl end
For humans,&nbsp;essential fatty acids have delta greater than {{c1::9}}
The {{c1::greater}} the length of the fatty acid, the {{c1::higher}} the melting point. The {{c1::more}} double bonds in a fatty acid, the {{c1::lower}} the melting point.&nbsp;More carbons = higher melting point<br>More double bonds = lower melting point
Triglyceride (triacylgylcerol) structure consist of a {{c1::glycerol}} linked to 3 fatty acids by {{c1::ester bonds}}"Formed by&nbsp;<b>dehydration</b>&nbsp;reaction<br><img src=""paste-af54362cb613247e65082fb69eec561a77b47b6e.jpg"">"
Where are triglycerides found? (2 locations)<u>Subcutaneous</u> (beneath the skin)<br><u>Visceral</u> (around internal organs)
Eicosanoids function as {{c1::signaling molecules}}. Ex. prostacyclins, prostaglandins, and thromboxanes<br>Made by oxidation of fatty acids<br>
Steroids are hormones synthesized from {{c1::cholesterol}}<br>Have <b>anti-inflammatory, immunosuppressant, metabolic, and endocrine effects</b>
Cell membranes regulate {{c1::intracellular composition}}
Cell membranes are preodominantly composed of {{c1::glycerophospholipids}}, {{c1::spingolipids}}, {{c1::glycolipids}}, and <i>cholesterol</i><br>Non-polar chains of phospholipids form the bilayer
{{c1::Micelles}} form when single-tailed fatty acids are placed in aqueous environments"<img src=""paste-044ba9bfff9b2a8c360f32e2fd19ee2f1a000a2a.jpg"">"
{{c1::Bilayer}} forms when two-tailed phospholipids are placed in an aqueous environment"<img src=""paste-50d0e84ab2a7e5ca0b0fbfd7fba94b174eb418ac.jpg"">"
{{c1::Liposomes}} form when lipids that constitute the bilayer are placed in an aqueous environment"<img src=""paste-50d0e84ab2a7e5ca0b0fbfd7fba94b174eb418ac.jpg"">"
COVID-19 mRNA vaccine delivered via {{c1::liposomes}}
{{c1::Liposomes}} are <u>lipid vesicles</u> that can deliver contents to cells via membrane fusion"<img src=""paste-50d0e84ab2a7e5ca0b0fbfd7fba94b174eb418ac.jpg"">"
Lipid movement across bilayer occurs {{c1::laterally}} while {{c1::transverse}}&nbsp;movement requires enzymes (non-spontaneous)"<img src=""paste-6442f2dc662b603755783ece405a3546a790005b.jpg"">"
Alaskan fish have more {{c1::unsaturated fatty acids}} , which lowers melting point
{{c1::Simple diffusion}} is the movement of materials <b>down a concentration gradient</b> from an area of high concentration to low concentration"Ex. O2, CO2, and CO<br><img src=""paste-13980e2a5deb22faa5e0e9639939b1b11ba4942c.jpg"">"
{{c1::Facilitated diffusion}} requires <b>transport proteins</b> such as aquaporins, ions, or glucose"<img src=""paste-50df9da1de8ef93a1738ff5963b1b517e40bee8e.jpg"">"
{{c1::Active transport}} needs energy to move molecules <i>against their concentration gradient</i>"Ex. Na+/K+ ATPase<br><img src=""paste-50df9da1de8ef93a1738ff5963b1b517e40bee8e.jpg"">"
Short chain fatty acids {{c1::acetate}}, {{c1::propionate}}, and {{c1::butyrate}} are the most abundant
{{c1::Short chain fatty acids}} maintain intestinal barrier integrity, influence production of mucus in GI tract, and protect from gut inflammation
"{{c2::<i>Propionate</i>}}<i>&nbsp;and&nbsp;</i>{{c2::<i>butyrate</i>}}&nbsp;inhibit activity of enzymes that are involved in a range of <b>neuropsychiatric disorders</b> including {{c1::depression}}, {{c1::schizophrenia}}, and {{c1::Alzheimer's disease}}"
Short chain fatty acids are involved in {{c1::gut-brain axis}} communication
{{c1::Cholesterol}} is built from isoprene and is a precursor for {{c2::fat-soluble vitamins (A, D, E, &amp; K)}}"<img src=""paste-8825e40b6fb22b82ed4b14cb46f07847f082990c.jpg""><br><img src=""paste-a9067d361afb3f00a75bc31820ae370096a49ce8.jpg"">"
{{c1::Apoptosis}} occurs when there are defects in membrane permeability or damage is caused by {{c2::<i>r</i><i>eactive oxygen species (ROS)</i>}}<br>ROS can cause <u>lipid peroxidation</u> and membrane damage
The {{c1::extrinsic apoptotic pathway}} is when signaling on the cell membrane activates <u>caspases, apoptosomes, and nucleases</u>
The {{c1::intrinsic apoptotic pathway}} is when <u>loss of mitochondrial cytochrome C</u> activates apoptosomes
Which fatty acid can be made in animal cells? <br>a. Linoleic acid <br>b. Oleic acid <br>c. Linolenic acid <br>d. Arachidonic acid <br>e. Eicosapentaenoic acid"B.<br><img src=""paste-d4eb6e33bf078c24edfecc394da0d42bf9894966.jpg"">"
Which fatty acid has the highest melting point? <br>a. Arachidic acid <br>b. Lauric acid <br>c. Myristic acid <br>d. Stearic acid <br>e. Palmitic acid"<i>A</i><br>More carbons = higher melting point<br><img src=""paste-031084418481c419929bd35c6c84a4e38ca37550.jpg"">"
Lipids are {{c1::amphipathic}}, meaning they have <b>polar and nonpolar components</b>. However, they have a <i>high proportion of hydrocarbons</i> in relation to other polar groups.
The main biological functions of lipids are<br>1. {{c1::Energy source}}<br>2. {{c1::Metabolism cofactors}}<br>3. {{c1::Structural components of membranes}}<br>4. {{c1::Cell signaling mediators}}<br><br>1. Energy source (fat)<br>2. Metabolism cofactors (vitamins)<br>3. Structural components of membranes (phospholipids)<br>4. Cell signaling mediators (cholesterol, cholesterol derived steroid hormones)
Of the saturated fatty acids, {{c1::arachidic}} acid has the highest melting point due to having {{c1::20}} carbons"<img src=""paste-dda5761321289986af1687734b07e344b0e9e1f1.jpg"">"
The Na/K ATPase is an example of which type of transport process? <br>a. Passive diffusion <br>b. Facilitated diffusion <br>c. Co-transport <br>d. Primary active transport <br>e. Secondary active transport<i>D</i><br>Directly uses ATP
What is the precursor to cholesterol? <br>a. Oleic acid <br>b. eicosanoids <br>c. corticosteroids <br>d. isoprenoids <br>e. propionate<i>D</i><br>Isoprenoids are precursors to cholesterol, which is a precursor to steroid hormones
In amino acids, the alpha-carbon is connected to an {{c1::amino}} group, {{c1::carboxyl}} group, {{c1::H atom}}, and {{c1::R}} groupR group defines amino acid characteristics and properties
Most of the amino acids found in living organisms are of {{c1::L}}-configuration because only {{c1::L-amino acids}} are incorporated into proteins
The {{c1::isoelectric point (PI)}} of an amino acids is the point at which the amino acid has a net charge of 0
Name the essential amino acids"<img src=""paste-be57606adc935613cb566f6d1e50008912a54c10.jpg"">"
{{c1::Polar side chains}} are usually on the surface of proteins due to their <b>hydrophilicity</b>&nbsp;S, Ser, Serine<br>T, Thr, Threonine<br>Y, Tyr, Tyrosine
{{c1::Quaternary structure}} is the assembly of multiple proteins with other moleculesEx. Hemoglobin, Ribosome<br>Same interactions that are in tertiary structure hold quaternary structure together
Examples of quaternary structure are {{c1::hemoglobin}} (protein + protein) and {{c1::ribosomes}} (protein + DNA/RNA)
{{c1::Soluble proteins::type of protein}} can have hydrophobic centers and hydrophilic exteriors to interact with water"<img src=""paste-ed72b566366883faffbb247ade7e4b13d7795cd0.jpg"">"
{{c1::Membrane bound proteins::type of protein}} have hydrophobic residues in fatty acid center of the lipid bilayer and hydrophilic residues outside of the lipid bilayer"<img src=""paste-222cdfc4e644c5257b5e9594daf92ca79e76d422.jpg"">"
Denaturation is the disruption and possible destruction of {{c1::secondary and tertiary}} structureProtein unfolding is caused by <i>disruption of homeostatic conditions<br></i>Primary structure remains intact
Denaturation is caused by:<br>1. {{c1::heat}}<br>2. {{c1::organic compounds}}<br>3. {{c1::detergents}}<br>4. {{c1::chaotropic agents}}<br>5. {{c1::salt}}<br>6. {{c1::pH}}
Heat (thermal energy) causes denaturation by disrupting {{c1::hydrogen bonds}}
{{c1::Organic compounds (urea)}} causes denaturation by <i>breaking disulfide bonds and altering the H-bonds of water</i>Extreme polarity of urea is responsible for this
{{c1::Detergents}} cause denaturation by <b>solubilizing hydrophobic groups</b>
{{c1::Chaotropic agents}} cause denaturation by <i>weakening</i> the hydrophobic effect<br>Chaotropic weakens<br>Detergents solubilize
Salt causes denaturation by {{c1::interrupting hydrogen bonds}}
{{c1::Changes in pH}} can denature proteins by changing the charge of a protein (R group side chains)
Protein folding begins <b>co-translationally</b> and is governed by {{c1::thermodynamics}} to achieve the {{c1::lowest free energy conformation}}<br>Must be folded into a certain shape to be functional<br>Identical protein sequences can have different functional shapes depending on environment<br>Different protein sequences can have the same shape
{{c1::Sickle cell anemia}} is a disease caused by a point mutation in the <i>6th amino acid of beta globin </i>from {{c1::glutamic acid (hydrophilic)}} to {{c1::valine (hydrophobic)}}"<br>Leads to misfolded hemoglibin and forms strands that make RBCs look like a sickle<br><img src=""paste-abf8d0abcbe9dab1de1df302bf029d68d482c793.jpg"">"
{{c1::Prion disease}} is <i>neurodegenerative disease</i>&nbsp;in which when a toxic form of prion proteins ({{c1::PrPsc}}) causes normal prion forms ({{c1::PrPc}}) to convert into the toxic form<br>Leads to polymerization of <u>amyloid fibers (plaques)</u>
Toxic prions are not attacked by the immune system because {{c1::there is no change in protein sequence}}
In prion disease, misfolded proteins accumulate to form new {{c1::beta strand interactions}} that lead to a polymerization into {{c1::amyloid fibers}}, which form <b>plaques</b> as seen in neurodegenerative diseases
Examples of <u>human prion diseases</u> are {{c1::Kuru (spongiform in cerebellum)}} and {{c1::Creutzfelt-Jakob Disease (CJD)}}
Which of the following is true regarding protein denaturation reactions? <br><br>a. Peptide bonds are broken and the primary structure is not retained <br>b. Denaturation disrupts (and even destroys) secondary and tertiary structures <br>c. Ammonium sulfate decreases melting temperature which favors denaturation <br>d. Denatured proteins retain some of their activity <br>e. Proteins can only be denatured in response to low pH<i>B</i>
Which of the following amino acids is NOT essential <br>a. Lysine <br>b. Threonine <br>c. Serine <br>d. Valine <br>e. Histidine"<i>C</i><br><img src=""paste-caffbe67f86f0e4069008cf95bc5ac0ecc8f4dc0.jpg""><i><br><br></i>"
{{c1::Plasma}} retains fibrinogen while {{c1::serum}} has no fibrinogen"<br>Anticoagulant <i>Heparin</i> is used for plasma, but not when serum is created<br>No anticoagulant = no fibrinogen in top serum layer<br><img src=""paste-610256d7162fb68c96301a7066b6fe0642bb96e8.jpg"">"
Albumin is synthesized in the {{c1::liver}} and secreted into {{c1::the blood}} when mature
Albumin <i>does not</i> contribute as much to blood viscosity due to {{c1::its ellipsoidal shape}}<br>Opposite of <u>fibrinogen</u>, which is elongated and contributes to viscosity
Albumin can function as a buffer due to its {{c1::16 histidine residues}}
{{c1::Hypoalbuminemia}} is caused by <b>liver cirrhosis, malnutrion, nephrotic syndrome, burns, and malabsorption</b>"<img src=""paste-9752b6ed3f160a5294c2201335004c4a2a8d72b6.jpg""><br><img src=""paste-950b4f62bb6ef3df24fd72f9f7462d6191520a2e.jpg"">"
{{c1::Hypoalbuminemia}} is characterized by a<b> drop in serum calcium and edema</b> (swelling caused by fluid retention in body tissues)<br>Fluid depletion in blood due to retention in tissues
Alpha and beta globulins are made in {{c1::the liver}}, while gamma globulins are made in {{c1::B cells/plasma cells}} during chronic infections
Cigarette smoking causes {{c1::Inactive alpha-1 antitrypsin}} by modifying the {{c1::methionine}} residue into {{c1::methionine sulfoxide}}. Because of this, macrophages release active/uninhibited <u>elastase&nbsp;that destroys the extracellular proteins of lung cells</u>, leading to {{c1::emphysema (destruction of lung alveoli)}}
{{c1::Transferrin}} is a beta globulin glycoprotein that <b>binds iron Fe3+</b> and transports it from {{c1::gut}} to {{c1::bone marrow}}
{{c1::Iron deficiency anemia}} is when the <i>free transferrin/bound transferrin ratio is high</i>, meaning transferrin is <b>less saturated</b> with ironTransferrin levels increase (also in 9/10 months of pregnancy)
{{c1::Hemochromatosis (iron overload)}} is when the <i>Free transferrin/bound transferrin ratio is low</i>, meaning there is greater transferrin-bound ironTransferrin is <b>saturated</b>
The gamma globulins are (5) {{c1::IgG (monomer), IgA (dimer), IgM (pentamer), IgD, and IgE}}<br>Gigantic Alpacas Manhandled Doorknobs Encouragingly<br>GAMDE
"<img src=""paste-9716fe851120c9f3c609ad4d1e63c38742e64af1.jpg""><br>What is the clinical condition given the above?""Monoclonal Gammopathy (Multiple myeloma AND Waldenströms macroglobulinemia)<br>Abnormal proteins (antibodies) are found in the blood<br><img src=""paste-0d416fd76da2b6e32ca50807691f6299c30d8c03.jpg"">"
"<img src=""paste-a2e6e1d858279d7b55539a402201776b55e139a3.jpg""><br>What is the condition given the above?"Multiple Myeloma<br>Sharp M band
In multiple myeloma,&nbsp;{{c1::Bence-Jones protein}} levels are high in urine, which means there is a <u>high level of light chain immunoglobulins</u>"<img src=""paste-ff6cb96b24b922193b98d725bf074862e590a4a2.jpg""><br>Characterized by sharp increase in M band"
"<img src=""paste-7ad306f2f58752994981cfbc0231cfd2ef494192.jpg""><br>What is the clinical consideration given the above? (dotted line indicates normal)""Cirrhosis of Liver<br><img src=""paste-87ea505bf692a542cebb4cfc9ce632832a28a4ce.jpg""><br><img src=""paste-40b401b6fb4b16aab096dddc42a69d9f1c4d266a.jpg"">"
"<img src=""paste-60dab4c5ab366b37ed5508491a97c26f7a4d2970.jpg""><br>What is the clinical consideration given the above?""Nephrotic syndrome<br><img src=""paste-5308f5d9dd5c6165e7bebff065f44172708e1b4a.jpg""><br><img src=""paste-630e3f6cec95fedd72cfae5a7c75d01cd9633ddc.jpg"">"
{{c1::C-reactive protein}} and {{c1::alpha 1-antitrypsin}} protein levels <i>increase</i> during inflammation and neoplastic (cancerous) conditions&nbsp;<br>Other proteins that increase:<br><b>Alpha 2-macroglobulin<br>Ceruloplasmin<br>Alpha-1 acid glycoprotein</b>
{{c1::Albumin}} and {{c1::transferrin}} protein levels <i>decrease</i> during inflammation and neoplastic (cancerous) conditions<br>Other proteins that decrease:<br><b>Transthyretin<br>Retinol binding protein</b>
In hyperproteinemia and hypoproteinemia, the abumin/globulin <u>ratio</u> {{c1::stays the same::increases, decreases, or stays the same}}
In {{c1::hyperproteinemia}}, both albumin and globulin levels are <i>high</i> in the blood<br>May be seen in <b>dehydration</b> due to inadequate water intake<br>A/G ratio stays the same
True or False?<br>In iron deficiency anemia, the free transferrin/bound transferrin ratio is low.<i>False</i><br>Iron deficiency anemia means there is not enough iron-bound transferrin (transferrin is less saturated with iron), so free transferrin/bound transferrin ratio is high
Which of the following acute phase proteins increases during an inflammatory reaction? <br>a. Albumin <br>b. Retinol binding protein <br>c. C reactive protein <br>d. Transferrin <br>e. Transthyretin<i>C<br></i>C reactive protein and Alpha 1-antitrypsin increase
{{c1::Enzymes}} act as catalysts that accelerate rate of reaction <u>without altering equilibrium of the reaction, being consumed, or being permanently altered.</u>&nbsp;
Enzymes reduce the {{c1::activation energy}} of a reaction to <b>increase the rate of reaction</b> by providing a more energetically favorable pathway"<img src=""paste-d85f0d4bfac5c34eced841e265afbee0d1c0a911.jpg""><br><img src=""paste-e6b9cc2f2d97926584be22fd38168b0400fee5be.jpg"">"
Most enzymes are {{c1::proteins}}, but some are RNA and are called {{c1::ribozymes}}
Active sites of enzymes can be {{c1::Lock &amp; Key}} model or {{c1::induced fit}} modelActive site residues can be <b>amino acids, cofactors, or RNaseH</b>
{{c1::Thiamin pyrophosphates (TPP)}} are made from <i>Vitamin B1 (Thiamin)</i> and used as a coenzyme by {{c1::pyruvate dehyrdogenase}}
{{c1::Riboflavin-P and FAD+/FADH2}} are made from&nbsp;<i>Vitamin B2 (Riboflavin)</i>&nbsp;and used as a coenzyme by {{c1::succinate dehyrdogenase}}
{{c1::NAD+/NADH and NADP+/NADPH}} are made from&nbsp;<i>Vitamin B3 (Niacin)</i>&nbsp;and used as a coenzyme by {{c1::lactate dehyrdogenase}}
{{c1::5’-Phosphopantetheines}} are made from&nbsp;<i>Vitamin B5 (Pantothenate)</i>&nbsp;and used as a coenzyme by {{c1::Acyl carrier protein (ACP)}}
{{c1::Pyridoxal Phosphate}} are made from&nbsp;<i>Vitamin B6 (Pyridoxine)</i>&nbsp;and used as a coenzyme by {{c1::Transaminase}}
{{c1::Biotin}} are made from&nbsp;<i>Vitamin B7 (Biotin)</i>&nbsp;and used as a coenzyme by {{c1::Acetyl CoA carboxylase}}
{{c1::Charged tetrahydrofolate}} are made from&nbsp;<i>Vitamin B9 (Folic Acid)</i>&nbsp;and used as a coenzyme by {{c1::Thymidylate synthase}}
{{c1::Adenosyl or Methylcobalamin}} are made from&nbsp;<i>Vitamin B12 (Cobalamin)</i>&nbsp;and used as a coenzyme by {{c1::Methyl malonyl CoA mutase}}
Vitamin B1 = {{c1::Thiamin}}
Vitamin B5 = {{c1::Pantothenate}}
Vitamin B6 = {{c1::Pyridoxine}}
Vitamin B7 = {{c1::Biotin}}
Vitamin B9 = {{c1::Folic Acid}}
Vitamin B12 = {{c1::Cobalamin}}
{{c1::Oxidoreductases::enzyme class}} transfer electrons, alter oxidation state of reactants"<img src=""paste-4ea9af104e828bf088a790df3da895395a94072b.jpg"">"
{{c1::Transferases::enzyme class}} transfer a functional group from one molecule to another"<img src=""paste-fc319d84f3512c02bdbad2b608aa53c350249ee1.jpg"">"
{{c1::Hydrolases::enzyme class}} break down a covalent bond with water"<img src=""paste-09b61d8dd26bb8e5dc2db84b4e2056759ae0d0a8.jpg"">"
{{c1::Lyases::enzyme class}} dissociate molecules, break covalent bonds without water, or perform oxidation/reduction"<img src=""paste-2121c0aa0a18fb103469d54166154aaad2b2693a.jpg"">"
{{c1::Isomerases::enzyme class}} rearrange bonds within the same molecule"<img src=""paste-83de3c8d0fd7b08a384618ca2aafe94a7b7f5111.jpg"">"
{{c1::Ligases}} join two molecules together and forms covalent bonds"<img src=""paste-f10e8d5e83fab31f4b61e4c4babe5c8f23b7133a.jpg"">"
"Which enzyme class catalyzes the following reaction? <br><img src=""paste-74f072e8dd94014713d964a27852d578d02b79f7.jpg""><br>a. Oxidoreductase <br>b. Hydrolase <br>c. Lyase<br>d. Transferase <br>e. Ligase"<i>B</i><br>Water used to break a molecule apart
"Which enzyme class catalyzes the following reaction? <br><img src=""paste-33c6a281fe39fce6e0579e139f6bd65f16799120.jpg""><br>a. Oxidoreductase <br>b. Hydrolase <br>c. Lyase <br>d. Transferase <br>e. Ligase"<i>A<br></i>Pyruvate is reduced to lactate, NADH is oxidized to form NAD+ (forward reaction)
{{c1::Reducing sugars}} can switch between open and closed forms (cyclization)"<img src=""paste-42ebb193a78ae5b4ffd9ea175595c7504bf9e3cf.jpg"">"
{{c1::Hemiacetylation}} is <b>cyclization</b> of a molecule, while {{c1::hemiketylation}} is the <i>opening up</i> of a cyclic structure to a linear molecule"<img src=""paste-5a9fba6e27b993e07d85049059bef45591c3437e.jpg"">"
{{c1::Furanoses}} like fructose and ribose are 5 membered rings"<img src=""paste-84b594f39351a6d7734573afd41a4ea428c67e5c.jpg"">"
{{c1::Connective tissue}} holds, wraps, and binds biological components for <b>support, protection, and transport</b><br>Cells: fibroblasts, chondroblasts, osteoblast, adipose (“-blast” = immature cell type)<br>Gels/Ground Substances: glycosaminoglycans (GAGs), proteoglycans, glycoproteins<br>Fibers: Collagen (strong), Reticular (net like), Elastic (very stretchy)
{{c1::Type I collagen::collagen type}} is made up of <i>2</i> (alpha-1 chains) and <i>1</i> (alpha-2 chain)
{{c1::Type 1 collagen::collagen type}} is found in <i>skin, bone, tendons, blood vessels, and cornea</i>Both type 1 and type 3 are found in blood vessels
{{c1::Type 2}} collagen is made of up <i>3 (alpha-2 chains)&nbsp;</i>
{{c1::Type 2 collagen::collagen type}} is found in <b>intervertebral disc cartilage and vitreous body</b>
{{c1::Type 3}} collagen is made up of 3 (alpha-1 chains)
{{c1::Type 3 collagen::collagen type}} is found in <i>blood vessels and fetal skin</i>Type 1 and type 3 collagen is found in blood vessels
{{c1::Type 4}} collagen is made up of 2 chains of variant alpha-1 and 1 chain of variant alpha 2
{{c1::Type 4 collagen::collagen type}} is found in the <b>basement membrane</b>
{{c1::Hydroxyproline (Hyp)}} and {{c1::Hydroyxylysine (HyLys)}} are formed by posttranslational modification of proline and lysine <i>by Vitamin C (ascorbate) dependent hydroxylases (Prolyl Hydroxylase, PDH)</i>"Lack of vitamin C = Scurvy<br><img src=""paste-aa61946757cca1f87d7f469d708de230ca7d379a.jpg"">"
{{c1::Collagen}} is synthesized in <u>fibroblasts and related cell types of osteoblasts (bone) or chondrocytes of cartilages</u>, and secreted into extracellular matrix
{{c1::Ehlers-Danlos Syndrome}} is a connective tissue disorder characterized by <u>loose and stretchy skin and loose joints</u>"<img src=""paste-a4d214e168e4e9b09358444db3904d40cafa3713.jpg"">"
{{c1::Osteogenesis Imperfecta}} is <u>brittle bone syndrome</u> - bones that easily bend and fracture"<img src=""paste-c55abcf7d9a176500506e04d5562fd29d1e13538.jpg"">"
<b>Elastin</b> is a stretchy and elastic connective tissue found in {{c2::lungs}}, {{c2::walls of large blood vessels}}, and {{c2::stretchy/elastic ligaments}}
<b>Elastin</b> is made of {{c1::glycine}}, {{c1::alanine}}, {{c1::valine}}, and small amounts of {{c1::proline}} and {{c1::lysine}}<i>G</i>assy <i>A</i>crobats <i>V</i>ideotaped <i>P</i>residential <i>L</i>ife
<u>Keratins</u> are tough fibers found in {{c2::nails}}, {{c2::hair}}, {{c2::epidermal layers}}, and {{c2::cytoskeletal intermediate filaments}}
{{c1::Laminin}} are glycoproteins that awhen defective, can lead to <i>muscular dystrophy and skin blisters</i>
If n{{c1::&gt;::&gt;, &lt;, or =}}1 there is cooperative binding<b>Hemoglobin<br>Oxyhemoglobin<br>PFK-1</b>
If n{{c1::=::&gt;, &lt;, or =}}1 there is no cooperative binding<b>Myoglobin<br>Deoxyhemoglobin or fully saturated Hb</b>
Myoglobin has either {{c1::ferrous iron (Fe2+)}} which is a normal heme or {{c1::ferric iron (Fe3+)}} which cannot bind O2 as well"Ferric gives the ""ICK"" cuz it sucks and binding oxygen (compared to ferrous)"
"Hemoglobin in the {{c1::T (""taut"")}} state is {{c1::deoxyhemoglobin}} and has a l<i>ow affinity for oxygen&nbsp;</i>"
Hemoglobin in the {{c1::R (relaxed)}} state is {{c1::oxyhemoglobin}} and has a <i>high affinity for oxygen</i>
If n{{c1::&lt;::&gt;, &lt;, or =}}1, ligands that bind prevent more ligands from binding (negative cooperativity)
The {{c1::bohr effect}} occurs when <u>[H+] increases</u> in muscles, which causes <b>more O2 to be unloaded</b> from hemoglobin"A right shift<br>[H+] increase = pH decrease, which decreases hemoglobin affinity for O2<br><img src=""paste-253e0bf9f7fffeb8ed72c163d67b183acdba97a9.jpg"">"
The {{c1::haldane effect}} occurs when hemoglobin has a higher affinity for CO2 after unloading its O2"Transports the CO2 to the lungs<br><img src=""paste-bbf04eccdcc46404b36e37b92c6e3c1def86b229.jpg"">"
Right shifts will occur where hemoglobin needs to <b>give/release</b> oxygen, therefore a right shift is caused by {{c1::increased [H+]/decreased pH}}, {{c1::increased temperature}}, {{c1::increased CO2}}, and {{c1::increased 2,3 BPG (bisphosphoglycerate)}}"<img src=""paste-253e0bf9f7fffeb8ed72c163d67b183acdba97a9.jpg"">"
A left shift will occur when hemoglobin needs to <i>retain</i> O2 (decrease O2 unloading) such as when {{c1::P50 decreases}}Occurs in <i>fetal hemoglobin</i> because they need a higher affinity for O2 to accept O2 from the mother
<u>Fetal hemoglobin</u> is made up of 2 {{c1::alpha}} chains and 2 {{c1::gamma}} chainsEpsilon and zeta chains (embryonic) disappear 6 months before birth (3 months into pregnancy)
The switch from fetal gamma chains to adult beta chains in hemoglobin occurs {{c1::3 months into pregnancy/6 months before birth}}
<i>Hemoglobin A2</i> is a variant of hemoglobin composed of 2 {{c1::alpha}} chains and 2 {{c1::delta}} chainsA high amount of HbA2 is <b>pathologic</b>
In electrophoresis, blood with sickle cell anemia (HbS) will {{c1::travel further towards the cathode}}"Glutamic acid (-) in HbA is replaced with valine (non-polar hydrophobic) in HbS, so HbS will be more attracted to the negative end (cathode)<br><br><img src=""paste-9882def5ba20407ea25d096dbb22ba99e0037e65.jpg"">"
Blood from a carrier of sickle cell anemia will produce what electrophoresis results?"Carriers have <b>some HbA and some HbS</b>, so:<br>One band (HbA) closer to the anode (+), and one band (HbS) closer to the cathode (-)<br><img src=""paste-16d8406b7ca82d5b53beacd22427ee1388ad7b44.jpg"">"
Hemoglobin carries <b>nitric oxide (NO)</b> in the blood to make its {{c1::vasodilatory effects}} strongerNO reacts with the <u>cysteine on HbA beta chain</u><b> </b>to make <i>nitrosothiol<br></i>
Effects of nitric oxide (NO) on hemoglobin are <i>reduced</i> in {{c1::sickle cell anemia::disease}}
Which is a part of normal heme in myoglobin?<br>a. Fe2+<br>b. Ag+<br>c. Cu3+<br>d. Cu2+<br>e. Fe3+<i>A.</i> Fe2+ (ferrous iron)
A 4 yo male presents to your office with evidence of growth retardation, chipmunk face, mild anemia. Genetic and gel-electrophoresis tests confirm a diagnosis of beta-thalassemia. What globulin groups make up HbA2?<br><br>a. α2β2<br>b. α2δ2<br>c. Β2δ2<br>d. ζ2ε2<br>e. α2γ2<i>B.</i> a2δ2<br>2 alpha and 2 delta chains
Which structure has the highest hill coefficient?<br>a. myoglobin<br>b. G3P dehydrogenase<br>c. Hemoglobin<br>d. PFK-1<br>e. 2,3 BPG"<i>C.</i> Hemoglobin<br>Hemoglobin demonstrates cooperative binding which means n&gt;1 (hemoglobin's is n=3)"
RBCs have an enyme called {{c1::carbonic anhydrase}} that <b>converts CO2 into bicarbonate </b>to be transported from muscles to the lungs (also occurs in kidneys)Occurs after haldane effect to take CO2 from muscles to lungs
There are 4 ways CO2 is transported from muscles to lungs:<br>1. converted to {{c1::bicarbonate}}<br>2. CO2 bound {{c1::directly to deoxyHbA}}<br>3. CO2 bound to {{c1::N-terminus of hemoglobin}}<br>4. dissolved in {{c1::plasma}} as gas<br>
What is the shape of the myoglobin-oxygen binding curve?<br>a. sigmoidal<br>b. linear<br>c. sinusoidal<br>d. exponential<br>e. hyperbolic"E. hyperbolic<br>Does not demonstrate cooperative binding, so isn't sigmoidal like hemoglobin<br><img src=""paste-04c678f4891da742014eff38672987788dbf854b.jpg"">"
Which change would increase the ability of hemoglobin to unload oxygen at tissues?<br>a. Increased pH<br>b. Increased 2,3 BPG<br>c. Increased HCO3 concentration<br>d. Decreased H concentration<br>e. Decreased lactic acid concentration<i>B.</i> increased 2,3 BPG<br>BPG binds to Hb to disrupt the bond between Hb and oxygen and release oxygen
Which amino acid binds to the proton produced via carbonic anhydrase in an erythrocyte?<br>a. Armenaine<br>b. Histidine<br>c. Proline<br>d. Glycine<br>e. lysine"B. histidine<br><img src=""paste-cc4beed48e59926cd9fdafcf193d8569961e754e.jpg"">"
An infant presents to your office with painful swelling of the hands and feet. Gel electrophoresis of hemoglobin demonstrates the patient only has HbS. What is the most accurate statement of this patient’s case?<br><br>a. The patient is considered a sickle cell trait carrier<br>b. This condition involves a mutation from valine to glutamic acid<br>c. The single band moved further towards the anode<br>d. The patient has elevated levels of HbA2<br>e. The patient’s RBC shape will be altered due to hydrophobic residues<i>E.</i> The patient’s RBC shape will be altered due to hydrophobic residues<br><br>Glutamate (-) is converted to valine (hydrophobic) which causes sickle shape<br>Not <i>A.&nbsp;</i>because carriers have both HbA and HbS
{{c1::Luft Disease}} is a defect in proper <b>mitochondrial oxygen utilization</b>
{{c1::Gout}} is characterized by the <u>formation of crystals</u> from elevated {{c1::urate}}, which damages the lysosome membrane resulting in the <i>release of degradative enzymes</i> <i>causing autolysis</i> of cells
{{c1::Wolman’s Disease}} is an autosomal recessive <i>lysosomal acid lipase deficiency</i>
{{c1::Zellweger Syndrome}} is a autosomal recessive disease characterized by <b>decreased levels of&nbsp;</b>{{c2::plasmalogens}}<b>, increased levels of&nbsp;</b>{{c2::long chain fatty acids}}<b>&nbsp;and&nbsp;</b>{{c2::cholastenoic acid derivatives}}<b>&nbsp;(bile acid precursors)</b>. The deficiency is due to the<br>absence of {{c1::functional peroxisomes}}
{{c1::Cystic Fibrosis}} is a mutation in <i>chloride channels</i> that keeps the channel closed, maintaning a <i>high concentration of intracellular Cl-</i>&nbsp;
In <u>cystic fibrosis</u>, high intracellular levels of Cl- cause an increased {{c1::Na+}} uptake from <i>airway lumen into cell</i>, causing {{c1::accumulation of mucus in airways}}
{{c1::Diastrophic Dysplasia (DTD)}} is a disease resulting from a <i>defect in sulfate transporter</i>, which causes low intracellular concentration of sulfate
In {{c1::Diastrophic Dysplasia (DTD)}}, low intracellular levels of <i>sulfate</i> lead to {{c2::under-sulfated cartilage and bones}}<br><br>Causes deformity in skeletal system
Dietary glucose is absorbed through the intestinal epithelium and transported by the {{c1::portal vein}} into organs
{{c1::GLUT 1}} transports glucose in&nbsp;<i>RBCs and the brain</i> (Km ~ 1mM)
{{c1::GLUT 2}} transports glucose in the <u>liver and pancreas</u> (Km ~15mM)Insulin made and secreted by <i>beta pancreas cells</i> activate GLUT 2 and facilitates liver glucose uptake
{{c1::GLUT 3}} transport glucose in most tissues (Km 1mM)
{{c1::GLUT 4}} transports glucose in <b>skeletal muscle and adipose</b> (Km ~5mM)
High <i>insulin</i> levels activate {{c1::Phosphofructokinase 2 (PFK 2)}}, which converts <u>{{c2::fructose 1,6 bisphosphate}} to {{c2::fructose 2,6 bisphosphate}}</u> in order to activate/upregulate {{c1::phosphofructokinase 1 (PFK1)}}F2,6BP upregulates PFK-1 to rev up glycolysis <br>PFK-1 is a rate-limiting step (F6P to F1,6BP)
Phosphofructokinase 2 (PFK-2) is activated by {{c1::insulin}} and inhibited by {{c1::glucagon}} through {{c1::cAMP kinase}}
When blood glucose is low, glucagon is {{c1::high}}<br>Glucagon activates cAMP kinase to phosphorylate pyruvate kinase (inactivating it)
When glucagon levels are high, glucagon activates {{c1::cAMP kinase}} to phosphorylate and inactivate {{c1::pyruvate kinase}} to <i>decrease the rate of glycolysis</i><br>Glucagon is high when blood glucose is low, so glycolysis in cells is slowed to <i>retain glucose in the blood and/or allow for more important cells (ex. brain) to get the glucose first</i>
Hemolytic anemia is caused by {{c1::glycolytic pyruvate kinase deficiency}}<br>Increase in 2,3 BPG lowers hemoglobin affinity for O2, leading to chronic hemolysis
The {{c1::Warburg effect}} is the increase in rate of glucose uptake and production of lactate <i>even in the presence of oxygen (normoxia)</i>Anaerobic glycolysis occurs even though there is available O2
In the <u>Warburg effect</u>, cancer cells phosphorylate and inactivate <b>pyruvate dehydrogenase</b> by using {{c1::pyruvate dehydrogenase kinase}}. This causes {{c1::lactic acid}} build up in the ECM, which acidifies the ECM to promote {{c1::tumor survival}}.&nbsp;<br>Lactic acid builds up in cell and leaves to ECM, which leads to a tumor microenvironment
In the {{c1::Warburg effect}}, increased acidity caused by l<u>actic acid buildup in the ECM</u> creates a tumor microenvironment in which <b>hypoxia and cancer</b> are promoted. Increased hypoxic conditions activate transcription factor {{c1::hypoxia inducible factor 1-alpha (HIF-1alpha)}} to promote uncontrolled cancer cell proliferation.
{{c1::Formic acid::saturated fatty acid}} has 1 carbon&nbsp;
{{c1::Acetic acid::saturated fatty acid}} has 2 carbons
{{c1::Propionic acid::saturated fatty acid}} has 3 carbons
{{c1::Butyric acid::saturated fatty acid}} has 4 carbons
{{c1::Caproic acid::saturated fatty acid}} has 6 carbons
{{c1::Caprylic acid::saturated fatty acid}} has 8 carbons
{{c1::Capric acid::saturated fatty acid}} has 10 carbons
{{c1::Lauric acid::saturated fatty acid}} has 12 carbons
{{c1::Myristic acid::saturated fatty acid}} has 14 carbons
{{c1::Palmitic acid::saturated fatty acid}} has 16 carbons
{{c1::Stearic acid::saturated fatty acid}} has 18 carbons
{{c1::Palmitoleic acid::unsaturated fatty acid}} is 16:1 (9)"<img src=""paste-4c8496d67dbb64da41ee898e531c4b97fd8764e2.jpg"">"
{{c1::Oleic acid::unsaturated fatty acid}} is 18:1 (9)"<img src=""paste-5cab27f4de9388727c8fefa3a0a075452c71d600.jpg"">"
{{c1::Linoleic acid::unsaturated fatty acid}} is 18:2 (9, 12)"<img src=""paste-baff7c81f8e044a3bcc96ff77efc719954aac027.jpg"">"
{{c1::Linolenic acid::unsaturated fatty acid}} is 18:3 (9, 12, 15)"<img src=""paste-5996b9e9d2ac25a3151f0b93419b9f5c726430a8.jpg"">"
{{c1::Arachidonic acid::unsaturated fatty acid}} is 20:4 (5, 8, 11, 14)"<img src=""paste-c5ce7d9cdb2f04478d0a3a2033fd1fe75660cb84.jpg"">"
{{c1::Long term control}} regulation usually occurs during development (synthesis, tissue formation) and takes <i>several hours to days</i><br>DNA--&gt;mRNA--&gt;protein<br><u>Ex. altering rate of enzyme synthesis</u>
{{c1::Short term control}} regulation is when active enzymes are temporarily regulated by <i>post-translational phosphorylation (kinases) or dephosphorylation (phosphatases)</i><br>Can take hours<br>Phosphorylation can either <b>activate or deactivate</b> depending on the enzyme
{{c1::Very short term control}} regulation is mediated by <i>allosteric regulators (metabolites)</i> and takes seconds to minutes"<br>Exhibits <u>sigmoidal</u> kinetics<br><img src=""paste-d8b5f4c8e88b089c35f4b071250a53d9d881e8ac.jpg"">"
{{c1::Glucagon}}, {{c1::epinephrine}}, and {{c1::cortisol}} <b>stimulate</b> gluconeogenesis while {{c1::insulin}} <i>inhibits</i> gluconeogenesis
<b>Gluconeogenesis</b> is important for organs that require a continues supply of glucose such as the {{c1::brain}}, {{c1::kidney}}, {{c1::RBCs}}, {{c1::cornea}}, and {{c1::lens}}
The substrates of gluceneogenesis are:<br><br>{{c1::Lactate (from anaerobic glycolysis)}}<br>{{c1::Glycerol 3 phosphate (from triacylglycerol)}}<br>{{c1::Gluconeogenic amino acids}}<br><i><br>Acetyl CoA is NOT a glucogenic substrate</i><br>Propionyl CoA from odd FA degradation can be converted to succinyl CoA, which becomes oxaloacetate through TCA cycle (OAA can enter gluconeogenesis)
All of the amino acids except for {{c1::leucine (L)}} and {{c1::lysine (K)}} are gluconeogenic amino acids
In gluconeogensis, <u>pyruvate carboxylase</u> is stimulated by {{c1::acetyl-CoA}}<br><br>
Pyruvate carboxylase requires {{c1::ATP}},&nbsp;{{c1::HCO3-}}, and&nbsp;{{c1::Biotin}}&nbsp;to convert pyruvate to oxaloacetate <b>in the mitochondria</b>
Phosphoenolpyruvate (PEP) carboxykinase is stimulated by {{c1::glucagon}} and {{c1::cortisol}} and requires {{c1::GTP}} to convert oxaloacetate to PEP <i>in the cytoplasm</i>
{{c1::Glucose 6 Phosphate dehydrogenase}} deficiency is the most common human enzyme deficiency<i><br>X-linked recessive</i>
<i>G6PDH deficiency </i>causes insufficient NADPH production and more reactive oxygen species (ROS)<br>ROS --&gt; RBC lysis --&gt; hemolytic anemia
The mutation in {{c1::G6PDH}} offers resistance to <i>malaria</i><br>More <i>oxidative stress</i> leads to parasitic resistance
Glucose 6 phosphate dehydrogenase is <b>activated</b> by {{c1::insulin}} and {{c1::NADP+}}
Glucose 6 phosphate dehydrogenase is inhibited by {{c1::NADPH}}
{{c1::NADPH}} is needed to reduce {{c1::glutathione}}, and r{{c1::educed glutathione}} is needed to convert <b>reactive oxygen species (H2O2)</b> to water (H2O)
{{c1::Chronic granulotmatous disease}} occurs when bacteria/viruses that carry {{c2::<u>catalase</u>}} break down {{c2::<i>hydrogen peroxide (H2O2)</i>}} that is used by the body to fight the bacteria<br>Patient potentially has G6PDH deficiency<br>Makes it difficult for patient to fight infection
Consumption of {{c1::fava beans}} are dangerous for with patients with <b>G6PDH deficiency</b> due to the oxidative stress
Oxidative stress, especially in patients with<i> G6PDH deficiency</i>, can damage RBCs to cause {{c1::hemolytic anemia}} or make RBCs look like {{c1::Heinz bodies}}&nbsp;
Increased metabolism in tumor cell proliferation cuases more {{c1::NADPH}} production, which increases {{c1::glutathione}} production to resist reactive oxygen species (ROS) and drug mechanisms<br>This prevents cell death<br><br><u>HIF-1a</u> is active under hypoxic conditions and activates G6PDH to fuel cell proliferation (tumor growth)
The cofactors of pyruvate dehydrogenase are {{c1::thiamine pyrophosphate (TPP)}}, {{c1::Lipoic acid}}, {{c1::HS-CoA}}, {{c1::FAD+}}, and {{c1::NAD+}}<br>T-rex Loves and Cares For Nachos<br><br>Pyruvate dehydrogenase is a <u>complex</u> of 3 principal enzymes, each with their own cofactors
Pyruvate dehydrogenase is a complex of 3 principal enzymes:<br><br>{{c1::Pyruvate decarboxylase}} (E1)<br>{{c1::Dihydrolipoamide acetyltransferase}} (E2)<br>{{c1::Dihydrolipoamide dehydrogenase}} (E3)
In the PDH complex, the cofactor of <u>pyruvate decarboxylase (E1)</u> is {{c1::thiamine pyrophosphate (TPP)}}
In the PDH complex, the cofactors of <u>dihydrolipoamide acetyltransferase</u><i> </i><u>(E2)</u>&nbsp;are {{c1::lipoic acid}} and {{c1::HS-CoA}}
In the PDH complex, the cofactors of <u>dihydrolipoamide dehydrogenase (E3)</u>&nbsp;are {{c1::FAD+}} and {{c1::NAD+}}
Pyruvate dehydrogenase is activated by {{c1::pyruvate dehydrogenase phosphatase}} and {{c1::calcium}}
Pyruvate dehydrogenase is inactivated by {{c1::pyruvate dehydrogenase kinase}} and inactivation is mediated by increased {{c1::acetyl-CoA}}, {{c1::NADH}}, and {{c1::ATP}}
Albumin has 4 major functions:<br><br>1. {{c1::Transport lipophilic molecules}}<br>2. {{c1::Regulate osmotic (oncotic) pressure}}<br>3. {{c1::Act as a buffer}}<br>4. {{c1::Nutrition}}<br>1. Transport lipophilic molecules (free FAs, steroid hormones, bilirubin, and ions)<br>2. Regulate osmotic (oncotic) pressure<br>3. Act as a buffer (due to its 16 histidine residues)<br>4. Nutrition (source of amino acids when hydrolyzed)
In {{c1::hypoproteiemia}}, both albumin and globulin levels are&nbsp;<u>low</u>&nbsp;in the bloodA/G ratio stays the same
Vitamin B2 = {{c1::Riboflavin}}
Vitamin B3 = {{c1::Niacin}}