Enclonar, Kimberly / MLS 3A
Enzymes
Lyases
Catalyze removal of groups from
substrates without hydrolysis; products
contain double bonds
Isomerase
Catalyze interconversion of geometric,
optical, or positional isomers
Ligases
Catalyzes the joining of 2 substrate
molecules
February 10, 2021
Glenn Charls Buelis, RMT, MLS (ASPIi)
Enzymes
• Specific biologic proteins that catalyze biochemical
reaction
• Not consumed in a reaction
• The substances in the reaction are converted into
products
• Act on substrate
• Have high specificity for their substrate
o Enzyme-Substrate relationship
• Present in trace amounts in blood and are subject to
saturation; released from degraded cells
o Enzymes are located intracellularly
• Found on all body tissues; found in serum in high
concentration after cellular injury
Terms to Remember
• Active Site
o Often a water-free cavity, where the substrate
interacts with a particular charged amino acid
residues
• Allosteric Site
o A cavity other than the active site
• Isoenzyme
o Different form of a particular enzyme; based on
certain properties (electrophoretic ability,
solubility)
o Based on location
• Isoform
o Result when an enzyme is subject to
posttranslational modifications
o Removal or addition of a component
• Zymogen/Proenzyme
o Structurally inactive form of enzyme
• Cofactor
o Non-protein molecule; necessary for enzyme
activity
o Activator - Inorganic cofactors, such as Cl or Mg
o Coenzyme - organic cofactor, such as NAD
• Prosthetic Group
o Coenzyme when bound tightly to the enzyme
o Apoenzyme - enzyme portion
o Holoenzyme - complete and active system
(APOENZYME+COENZYME)
Enzyme Nomenclature
• An enzyme's name usually corresponds with its
substrate and ends with the suffix -ase
• All enzymes are given numerical designation by the EC
of the International Union of Biochemistry
o EC 3.1.3.1 ALP
o EC 1.1.1.27 LDH
• 1st number - Classification
• 2nd 2 numbers - subclass & sub-subclass
• Last number - serial number
Enzyme Classification (OTHLIL)
Oxidoreductase Catalyze oxidation and reduction
reaction between 2 substrates
Transferases
Catalyze transfer of a group other than
hydrogen from one substrate to another
Hydrolases
Catalyzes hydrolysis of various bonds
Catalytic Reaction of Enzymes
• Lowers the activation energy that the reactants must
reach for the reaction to occur
o Activation energy/Free energy of activation energy required to start a reaction
• Rate of Reaction depends on activation energy/free
energy of activation
Enzyme Kinetics
• Lock and Key Model
o High degree of similarity between the active site
and substrate
• Induced-fit model
o Binding of the substrate induces a
conformational change in the enzyme
Factors that Influence Enzymatic Reaction
Substrate Concentration
• General enzyme, substrate, product relationship
o E + S → ES → E + P
• Substrate readily binds to a free enzyme at a ↓
substrate concentration
• Michaelis-Menten formula - a curve that shows the
relationship of reaction velocity to substrate
concentration
• Adding a substrate, ↑ rate of reaction, except if all
enzymes are saturated
Enclonar, Kimberly / MLS 3A
• First Order Kinetics
o The reaction rate varies directly with the
substrate's concentration with a fixed amount of
enzyme
• Zero order Kinetics
o The velocity of reaction is not affected by the
addition of more substrate at a certain point.
When maximum velocity is reached, the rate
increase in velocity is zero (zero order reaction).
Thus, rate of reaction depends on enzyme
concentration.
• Endpoint (Fixed-time method)
o Combines reactants, stops the reaction at a fixed
time and then measures the product formed
• Kinetic (Continuous monitoring)
o Combines reactants, then measures the change
in absorbance at a specific time interval over a
specific period of time
Enzymes
Enzyme Concentration
• As long as the substrate concentration exceeds the
enzyme concentration, the velocity of the reaction is
proportional to the enzyme concentration; ↑
enzyme, faster reaction
pH
• Enzymes are in its maximal activity at optimal pH (7.08.0)
Temperature
• ↑ temperature ↑ rate of reaction by increasing the
movement of molecules
• Every 10C ↑ - doubling of activity, until protein is
denatured
• At 65C = start of denaturation
Cofactors
• Activators and Enzymes
Inhibitors
• May act as reversible or irreversible inhibitors
(permanent attachment to enzyme)
• Competitive inhibitor
o Physically binds to the active site of an enzyme
and compete with the substrate for the active
site; can be reversed by increasing substrate
concentration
• Noncompetitive inhibitor
o Binds an enzyme at a place other than the active
site and may be reversible or irreversible
o Induces conformational change in the enzyme so
that the substrate cannot bind
• Uncompetitive Inhibitor
o Inhibitor binds to the ES complex - cannot be
reversed by adding more substrate
Enzyme Measurement
• Measure enzyme activity and reported in
International Unit (IU) or less commonly in kat (katal).
o 1 IU = 1 umol of substrate to produce/min
o 1 kat = 1 mol of substrate/sec
o 1 IU = 16.7 kat
• Enzyme activity is reflected by measuring the small
increase in product which is easier to do than
measuring small decrease in large amount of
substrate
• Rate of Reaction - rate of disappearance of reactants
or rate of appearance of products
• Enzyme reaction may be coupled with another
reaction where an indicator substance uses the
products producing another product which is
measured and reflects the amount of enzyme present
Alkaline Phosphatase (ALP)
• Non-specific enzyme capable of reacting with many
different substrates
• Optimal pH reaction is 9.0-10.0
• Activator: Mg2+
• Highest concentration in intestine, liver, bone, spleen,
placenta, kidney
• Isoenzymes
o Placental - most heat stable of all normal ALP
isoenzyme
o Intestinal - Least Anodal
o Liver - highest concentrations, most anodal
(fastest)
o Bone - most heat labile
o Carcinoplacental isoenzyme include Regan,
Nagao, and Kasahara (found in patients with
malignancy)
▪ Regan is the most heat stable
Clinical Significance
• Evaluation of hepatobiliary and bone disorders
• Cholestatis, hepatitis, and cirrhosis
• Highest elevation in Paget's disease (osteitis
deformans)
• Other bone disorders: osteomalacia, rickets,
hyperparathyroidism, and osteogenic sarcoma
• Children, adolescents, pregnant women have higher
values
• Usually found in bile canaliculi - increased in
blockages
Enclonar, Kimberly / MLS 3A
Methods
• Reference Value: 30-90 U/L (30C)
• 4 isoenzyme (electrophoresis migration)
o Isoenzyme separation: Acrylamide gel,
electrophoresis, chemical or heat (56C; 10mins)
o Liver → Bone → Placenta → Intestinal
• Heat Denaturation (Most heat stable to most heat
labile)
o Placenta → Intestinal → Liver → Bone
• Substrate: Organic phosphates such as B-glyceroPO4
and p-nitrophenylPO4
• Other Methods:
o Bodansky (B-glyceroPO4)
o Shinowara-Jones-Reinhart (B-glyceroPO4)
o King-Armstrong (phenylPO4)
o Bessy-Lowry-Brock (p-nitrophenylPO4)
o Bowers-McComb (p-nitrophenylPO4) - Most
specific; pH 10.15 @405nm
▪ PNPP → p-nitrophenol + PO4-
• Fewer amount in the kidney, pancreas and RBCs
• Isoenzymes: Cytoplasmic & Mitochrondrial
Clinical Significance
• Mainly in evaluation of hepatocellular disorders and
skeletal muscle
o Found in hepatocytes
• Increased in AMI within 6-8hrs; but not useful in
diagnosis of AMI
• Increased in viral hepatitis, cirrhosis, muscular
dystrophies, and inflammatory conditions
Methods
• Reference Value: 5-35 U/L
• Sources of error: Hemolysis can dramatically increase
serum AST
• Method: Karmen Method (uses malate
dehydrogenase) - pH 7.5, 340nm
Alanine Aminotransferase (ALT)
Acid Phosphatase (ACP)
• A hydrolase that catalyze the same type of reactions
with ALP
• Difference between ACP and ALP is the pH of reaction
• Optimal pH approximately 5.0
• Found in prostate (highest), bone, liver, spleen,
kidney, RBCs, and platelets
• Isoenzymes:
o RBC-ACP - inhibited by Copper
o Prostate-ACP (pACP) - inactivated by Tartrate
o Both differentiated using inactivation
Clinical Significance
• Aid in detection of prostatic carcinoma, particularly
metastatic carcinoma
• Not sensitive at early stage = prostate specific antigen
is preferred
• Proved useful in forensic CC: investigation of rape
(seminal fluid-ACP activity; persists for 4 days) >50
IU/L
Methods
• Reference Value:
o 2.5-11.7 U/L (Total ACP)
o 0-3.5ng/mL (Prostatic ACP)
• Very labile, add 5M acetate buffer or citrate tablet to
preserve
• Substrate: Organic phosphates such as B-glyceroPO4
and p-nitrophenylPO4
o Thymolphthalein monophosphate (most specific
substrate for pACP) - for quantitative endpoint
reactions (Roy and Hillman)
o A-napthyl phosphate - for continuous
monitoring
• Other Methods
o Gutman & Gutman (phenylPO4)
o Shinowara (p-nitrophenylPO4)
o Babson, Read, Philipps (a-napthylPO4)
Aspartate Aminotransferase (AST)
•
•
•
•
Belongs to the class of transferases
Formation of glutamate + oxaloacetate
Coenzyme: pyridoxal phosphate
Older term: serum glutamic oxaloacetic transaminase
(SGOT or GOT) - based on product
• Transaminase
• Highest concentrations are found in cardiac tissues,
liver and skeletal muscle
o Highest in cardiac tissues
• A transferase with enzymatic activity similar to that of
AST
• Catalyzes transfer of amino group from alanine to aketoglutarate with the formation of glutamate and
pyruvate
• Coenzyme: pyridoxal phosphate
• Older term: serum glutamic pyruvic transaminase
(SGPT or GPT)
• Highest concentration is in the liver which makes it
more specific for liver disease than AST
Clinical Significance
• Evaluation of Hepatic disorders
• Higher elevations found in hepatocellular disorders
than extrahepatic or intrahepatic obstructive
disorders
• Acute inflammatory conditions of liver = ALT elevation
is frequent than AST
• Highest in viral hepatitis
Methods
• Reference Value: 7-45 U/L
• Coupled Enzymatic Method
o LD as the indicator enzyme
o Change in absorbance at 340nm measured
continuously is directly proportional to ALT
activity
o Optimal pH 7.3-7.8
• Reitmen Frankel
o Alanine + a-ketoglutaric → pyruvic acid
o Addition of DNPH (2,4-dihydrophenylhydrazine)
to pyruvic acid to produce color
AST/SGOT
ALT/SGPT
Substrate
Aspartate aketoglutarate
Alanine aketoglutarate
End Product
Oxaloacetic acid
+ glutamate
Pyruvic acid +
glutamate
Location
Heart, Liver,
Skeletal Muscle
Liver, Heart
High Concentration
Heart
Liver
Significance
AMI
Liver disease
De Ritis Ratio
Viral Etiology
↑ ALT
ALT/AST >1
Non-viral
↑ AST
ALT/AST <1
Enclonar, Kimberly / MLS 3A
Amylase (Amy)
• Belongs to the class of hydrolase
• Smallest enzyme; catalyzes the breakdown of starch
and glycogen
• Activators: Calcium & Chloride
• Major tissue source: acinar cells of pancreas and
salivary glands
• Lesser concentrations: Skeletal muscle, intestine,
fallopian tube
• Pancreatic AMS: amylopsin
o Isoenzyme (P1, P2, P3)
o P2 - commonly observed fraction
• Salivary AMS: ptyalin
o S1, S2, S3
o S1 and S2 - commonly observed fraction
• Serum AMS: pancreatic in origin
o MicroAMS
▪ Unbound, free; 50,000 dal.
▪ Found in urine
o MacroAMS
▪ Bound to IgG, IgA; High MW
▪ Measured in serum
Clinical Significance
• Diagnosis of Acute pancreatitis - ↑ in P-type activity;
predominantly P3
• ↑ level in salivary gland lesions, such as mumps and
parotitis; perforated peptic ulcer, intestinal
obstruction, cholecystitis, acute appendicitis
• Earliest marker for acute pancreatitis
o Found within 5-8 hrs (as early as 2 hrs)
Methods
• Reference Value
o Serum: 28-100 U/L
o Urine: 1-15 U/h
• Saccharogenic
o Measures the appearance of the product
(glucose: Somogyi)
o Somogyi: mL glucose released in 30mins at 37C
• Iodometric/Amyloclastic
o Measures the disappearance of the substrate
(starch)
o Decrease in dark-blue: iodine
• Chromogenic
o Measures dye released from breakdown of
polysaccharide
o Measures ↑ color intensity from the production
of products coupled with a dye
Kinetic
•
o Coupling of several enzyme systems to monitor
amylase activity
o Measures change of NAD to NADH at 340nm
Lipase (Lps)
• Hydrolyzes the ester linkages of fats to produce
alcohols and fatty acids
• Breaks down Tag into fatty acids and glycerol
• Highest concentration in pancreas
• Lesser amounts in stomach and small intestines
• Isoenzymes: L1, L2, L3
o L2 - most clinically specific and sensitive
Clinical Significance
• Diagnosis of acute pancreatitis
o Serum LPS activity increase 4-9hrs after attack
o Concentration peak 24hrs
o Decrease within 8-14 days
• Most specific marker in diagnosing acute pancreatitis
Methods
• Reference Value: <38U/L
• Cherry-Crandall (reference method)
o Principle: Measures liberated fatty acids by
titration after a 24hrs incubation
o Substrate: 50% Olive oil (before); Triolein (more
pure form of TAG)
• Sigma-Tietz
• Titration
• Peroxidase-coupling - most common method used
now
Lactate Dehydrogenase (LDH)
• Enzyme that catalyzes the interconversion of lactic
acid and pyruvic acids
• Highest concentration: heart, liver, skeletal muscle,
kidneys, and RBCs
• Lesser amounts in lungs, smooth muscle, and brain
• Isoenzymes:
o LD1 (anodic)
o LD5 (cathodic)
o LD1 & LD2 - heat stable
o LD5 - most labile
o 4 subunits (tetramer)
o LD6 - alcohol dehydrogenase
• Do not refrigerate!
Isoenzyme
Tissue
Disorder
LDH-1 (HHHH)
Heart
RBCs
MI
Hemolytic anemia
LDH-2
(HHHM)
Heart
RBCs
Megaloblastic anemia
Acute renal infarct
Hemolyzed specimen
LDH-3
(HHMM)
Lung
Lymphocytes
Spleen
Pancreas
Pulmonary embolism
Extensive pulmonary
pneumonia
Lymphocytosis
Acute pancreatitis
Carcinoma
LDH-4
(HMMM)
Liver
Hepatic injury or
inflammation
LDH-5
(MMMM)
Skeletal muscle Skeletal muscle injury
Clinical Significance
• Increased levels in cardiac, hepatic, and skeletal
muscle and renal disease
• Least specific enzyme marker
• Highest level is seen in pernicious anemia and
hemolytic disorders
• Increased in: Viral hepatitis, cirrhosis, AMI, some
leukemias
• Marked elevation: Acute lymphoblastic leukemia
• Normal LD Isoenzyme concentration:
o LD2>LD1>LD3>LD4>LD5
• If LD1>LD2 (Flipped ratio/pattern) - suggestive of AMI
• Increased LD6 is seen in arteriosclerotic
cardiovascular failure
Methods
• Reference Value: 125-220 U/L
• Source of error: Hemolysis since RBS contain LD conc.
approximately 100=150x found in serum
• Interconversion of Lactic and Pyruvic acid using
coenzyme NAD+
Enclonar, Kimberly / MLS 3A
• Wacker Method (Forward/Direct Reaction) - pH 8.38.9 - measures pyruvate
• Wrobleuski La Due (Reverse/Indirect Reaction) - pH
7.1-7.4
o Faster
• Tanzer-Gilvarg (forward)
o ↓ absorbance of NADH to NAD at 340nm (pH
9.0)
o Uses additional pyruvate kinase and LDH
Creatine Kinase (CK)
• Other names: Creatine Phosphokinase (CPK); ATPcreatine-N-phosphotransferase
• Extracted from the Greek word kreas
• Identified in 1831 as a component of skeletal muscle
• Nitrogenous organic acid which supplies energy to the
cells and tissue
• Activator: Mg2+
• Catalyzes the reversible reaction in the formation of
ATP in tissues
• Creatine + ATP → creatine phosphate + ADP
• Found in heart, brain, skeletal muscles and others
• CK-BB (CK1)
o Brain type
o Small quantity in tissue
o Short half-life of 1-5hrs
o High concentration in the CNS
o "Blood-brain-barrier"
o "Tumor-associated marker"
• CK-MB (CK2)
o Predominant in cardiac tissue (major source)
o ≥6% increase of total CK is good indication of
myocardial damage
o Hybrid type
o Level rise: 4-8hrs after MI
o Peaks at: 12-24hrs
o Declines: 48-72hrs
o "time-frame" is crucial
• CK-MM (CK3)
o Muscle type
o Major isoenzyme of the serum (94-100%)
o Heart & skeletal muscle activity
o Increased due to:
▪ Hypothyroidism, cardiac, and skeletal
muscle injury
▪ Mild to strenuous activity
▪ Intramuscular injections
• Macro-CK2
o Migrates between CK2 and CK3
• CK-Mi
o Migrates slightly in opposite direction
o Point cathodal to CK-MM
Clinical Significance
• Increased in:
o AMI
o Muscular dystrophy: Duchenne type (50-100x
increase)
o Hyperparathyroidism
o Malignant hyperpyrexia
o Reye's syndrome
Methods
• Reference value:
o Male: 46-171 U/L
o Female: 34-145 U/L
o CK-MB: <5% total CK
• Electrophoresis
• Ion-exchange chromatography
• Immunoassays
o RIA
o Immunoinhibition methods
• Oliver-Rosalki (reverse)
o ↑ in absorbance at 340nm (pH 6.8)
o Uses additional hexokinase and G6PD
Gamma-Glutamyltransferase (GGT)
• Enzyme involved in the transfer of the y-glutamyl
residue from y-glutamyl peptides to amino acids,
H2O, and other small peptides
• Most sensitive enzyme for all types of liver disease
o Highest levels with obstructive disorders
• Tested with ALP to confirm obstructive disorder
• Marker for daily consumption of large amount of
alcohol or drugs
• Market for chronic alcoholism
• Found in: Kidney, Brain, prostate, pancreas, liver
Clinical Significance
• Increased in:
o Biliary tract obstruction
o Patient taking warfarin, phenobarbital, and
phenytoin (enzyme inducing drugs)
o Chronic alcoholism
o Pancreatitis, diabetes and MI
Methods
• Reference Value
o Male: 6-55 U/L
o Female: 5-38 U/L
• Szaz Method
o Substrate: gamma-glutamyl p-nitroanilide
o Measured at 405-420nm
o Principle: y-glutamyl residue is transferred to
glycylglycine, releasing p-nitroaniline, a
chromogenic product
5' Nucleotidase (5NT)
• Responsible for catalyzing the hydrolysis of
nucleoside-5'-phosphate esters
• Significantly elevated in hepatobiliary disease
• Secondary marker for obstructive jaundice
• More sensitive to metastatic liver disease than ALP
• Reference Value: 3-9U/L
Pseudocholinesterase (ChE)
• Secreted by the liver; representing synthetic function
• Marker for insecticide/pesticide poisoning
(organophosphate)
• Important in the cleavage of succinylcholine
• Only enzyme that is significant when ↓
• Method: Michael-Ellman
o Substrate: Acetylcholine
• Reference Value: 0.5-1.3 pH units (plasma)
Enclonar, Kimberly / MLS 3A
Reference Values
Breast cancer
RA
ALP
30-90 U/L
ACP
2.5-11.7 U/L (Total ACP)
0-3.5ng/mL (Prostatic ACP)
AST
5-35 U/L
ALT
7-45 U/L
Amy
Serum: 28-100 U/L
Urine: 1-15 U/h
CK
MI
Neuroleptic malignant
syndrome
Cysteine Cathepsins
Premalignant lesions in
colon, thyroid, brain, liver,
breast, and prostate
GGT
Premalignant lesions in
colon, thyroid, brain, liver,
breast, and prostate
Gelatinase-B
Cardiovascular mortality
Gastric cancer
Vascular dementia
RA
Malignant gliomas
Glycogen phosphorylaseBB
MI
G6P
Gierke disease
Hypoglycemia
G6PD
Gastric cancer
Non-enzymatic MI Markers
LDH
Myoglobin
• Major protein responsible for oxygen supply of
striated muscle
• Rapidly released into the bloodstream following
muscle injury due to its abundance in cardiac muscle
tissue and low molecular weight
Pyroptosis
Necrosis
Breast cancer
Leukocyte esterase
Periprosthetic joint infection
UTI
Bacterial peritonitis
Ascitic fluid infection
Lipase
Acute pancreatitis
Lysozyme
RA
Tuberculous meningitis
Tuberculous pericarditis
Tartrate-resistant acid
phosphatase
Osteoarthritis
Tartrate-resistant acid
phosphatase-5b
Giant cell tumor
Bone metastases
Lps
<38 U/L
LDH
125-220 U/L
CK
Male: 46-171 U/L
Female: 34-145 U/L
CK-MB: <5% total CK
GGT
Male: 6-55 U/L
Female: 5-38 U/L
5NT
3-9 U/L
ChE
0.5-1.3 pH units (plasma)
Acute Myocardial Infarction
Troponin
• The troponin complex is a component of the thin
filament of striated muscle linked to actin
• 3 subunits:
o Troponin I: an inhibitory subunit
o Troponin T: tropomyosin-binding subunit
o Troponin C: calcium - binding subunit
Enzyme
Disorder/Disease
ACP
Malaria
Prostatic carcinoma
ALT
Hepatocellular damage
Hepatitis B and C
ALP
Chronic kidney disease
Paget Disease or
rickets/osteomalacia
Type II diabetes
Obstructed liver
Amylase
Pancreatitis
MI
AST
Hepatic disease
Dental disorder
Liver fibrosis
Butyrylcholinesterase
Schizophrenia
Alzheimer's disease
Parkinson's disease
Cathepsin-D
Renal cell carcinoma
Dental disorder
Case Study 1
• Age: 40
• Chief complaints: Fever, vomiting, indigestion,
diarrhea, pain on the right side radiating to the lower
back up to the shoulders
• Lab results:
o WBC ↑
o Lipase N
o ALT, AST, ALP, Total Bilirubin ↑
• Disease: Hepatitis
Case Study 2
• Age: 39
• Chief complaints: The patient was brought to the
emergency department via ambulance due to
decreased level of consciousness, nausea, and
vomiting
• Lab results:
o ALT, AST normal
o Total Bilirubin, Lipase ↑
o Amylase ↑↑
Disease:
Acute pancreatitis
•
Enclonar, Kimberly / MLS 3A
Myoglobin
Trop T
Trop I
CK-MB
AST
LD
Elevation after 2-4 hrs (1st
chest pain (MI) nonenzyme/protein
to rise)
3-4 hrs
3-12 hrs
4-8 hrs (1st
enzyme to rise)
6-8 hrs
8-10 hrs
Peak Activity
6-10 hrs
48 hrs
12-24 hrs
12-24 hrs
24-48 hrs
72 hrs
Duration of
elevation
2-5 days
2-5 days
5-10 days
2-3 days
4 days
10 days
Sensitivity
(increase
immediately)/
Specificity
Sensitive but not
specific
More
sensitive and
specific than
CK-MB
More
sensitive and
specific than
CK-MB
Not entirely
specific MI
Not sensitive,
not specific
Insensitive,
nonspecific
Usefulness
Negative predictive
marker
More
sensitive and
specific than
CK-MB
More
sensitive and
specific than
CK-MB
Used to be the
"gold standard"
Used to detect
infarction >3
days prior to
testing
Used to detect
infarctions
occurred >5 days
prior to testing
Eliminates
need for LD
isoenzyme
Eliminates
need for LD
isoenzyme
Negative results
within first few
hours after chest
pain; rule out MI
Popularity is
declining due to
newer tests
Gold
standard
Methods
Latex agglutination
ELISA
Immunonephelometry
Fluoroimmunoassay
ELISA
ELISA
E'phoresis
RIA
Immunoinhibition
E'phoresis
Immunoinhibition
Troponin and CK-MB - recommended for MI
2 samples, maximum 3
• 1st sample - at presentation
• 2nd sample - after 6-9 hrs
• 3rd sample - after 12-24 hrs
MI according to Bishop (M Trop CAL <3)
Myoglobin
Trop T
Trop I
CK-MB
AST
LDH
Onset
2-3 hrs
-
-
4-8 hrs
6-8 hrs
12-24 hrs
Peak
8-12 hrs
-
-
12-24 hrs
24 hrs
48-72 hrs
Duration of Elevation
18-30 hrs
-
-
48-72 hrs
5 days
10 days
Disease Condition
Lab Findings
Alcohol Fatty Liver
Slight elevations of ALT, AST, GGT, with fatty infiltrates
Alcoholic Hepatitis
Moderate elevations of ALT, AST, GGT, ↑ Total Bilirubin, ↑ PT, ↓ Protein
Alcoholic Cirrhosis
Elevated ALT, AST, GGT, with gastrointestinal bleeding