MLS 311: Clinical Chemistry
Proteins
Clinical Chemistry I
Proteins
Objectives:
Upon completion of this lesson, the student will be able to:
Student Learning Outcomes:
Exercise independent judgement and critical thinking to correlate and recognize discrepancies
SLO #3
associated with normal and abnormal test results using patient history, characteristics, and
demographics.
Demonstrate effective oral or written communication with other students, faculty, patients,
SLO #5
professional colleagues, physicians, other members of the health care team, and the public to
effectively and efficiently transmit test results and instructions.
Demonstrate and value professional conduct that includes compassion, concern, integrity and
SLO #7
respect when dealing with patients, colleagues, faculty, students, physicians, other members of the
health care team and the public independent of race, sex, religion, ethnicity or diversity.
Practice and demonstrate the use of appropriate ethical standards in all matters related to medical
SLO #8
information and patient care including strict adherence to patient confidentiality rights as
mandated by the Health Insurance Portability and Accountability Act (HIPAA).
Cognitive:
C1:12
C1:13
C1:13A
C1:13B
C1:13C
C1:13D
C1:14
C1:15
C1:15A
C1:16
C1:17
C1:18
C1:19
C1:19A
C1:19B
C1:19C
C1:19D
C1:19E
C1:19F
C1:19G
C1:20
C1:20A
C2:3
C2:3A
C2:3B
C2:3C
C2:3D
Identify and differentiate proteins from other organic molecules based on their structure
including the presence of amine, carboxylic acid functional groups, and amino acids.
Define the levels of protein structure including the chemical interactions and molecules
involved in the formation and stabilization of the structure.
Primary (peptide bonds)
Secondary (hydrogen bonds, alpha helices and beta sheets)
Tertiary (protein domains, globular and fibrous, hydrophobic interactions, disulfide bonds, coiled
coils, barrels)
Quaternary
Define amphipathic and amphoteric as it relates to protein structure
Outline the process of protein digestion and absorption (metabolism).
Define diurnal and explain the effect on metabolism and protein concentrations.
Define proteins as simple, conjugated, and Apo proteins and provide examples of each.
Define hyperproteinemia and hypoproteinemia.
Define exudate and transudate.
Define the clinically significant serum proteins and their normal physiological role.
Pre-albumin [transthyretin] and retinol-binding protein [RBP]
Albumin
Alpha 1 globulins (alpha 1 antitrypsin, alpha 1 lipoprotein, alpha 1 fetoprotein, alpha 1 acid
glycoprotein, alpha 1 carcinoembryonic antigen [CEA]
Alpha 2 globulins (haptoglobin, alpha 2 macroglobulin, ceruloplasmin, alpha 2 lipoprotein)
Beta globulins (transferrin,C-reactive protein, complement factors, fibrinogen, beta-lipoprotein
Gamma globulins (IgM, IgG, IgA, IgE, IgD, Bence Jones proteins)
Proteins in other body fluids.
Define and differentiate protein chemical digestion and denaturation
List and explain chemical and physical factors that can denature, coagulate or alter protein
structure.
Explain and perform the methodologies used for quantitating total protein and clinically
significant individual proteins in serum and other body fluids including the chemical
principle, interfering substances and clinical use of each.
Kjedahl
Direct Photometric
Biuret (urine, serum)
Dye-Binding (urine, serum)
Revised 10/10/2023
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MLS 311: Clinical Chemistry
Proteins
C2:3F
C2:3G
C2:4
C2:7
C2:19
C2:24
C4:12
C4:12:G
C4:157
C4:158
Affective:
G1:1G1:4L
Refractometry
Turbidometric or Nephelometric
Define chromatography, column chromatography, derivitization, mobile phase, resolution,
detector, retention factor, retention time, stationary phase and planar chromatography.
Describe and differentiate internal standard, ion exchange, partition, adsorption, steric
exclusion, thin-layer and affinity chromatography including principles of separation,
stationary and mobile phases, and clinical applications.
Define the following terms in association with mass spectrometry: base peak, ion trap, mass
analysis, mass-to-charge ratio, molecular ion, product/fragment ion, proteomics and timeof-flight.
Define the following: agarose, ampholyte, amphoteric, blot/blotting, densitometry,
electroendosmosis, electrophoresis, electrophoretic mobility, polyacrylamide and wick flow.
Define the clinical significance of proteins in other body fluids including reference range
and quantitation
Fetal fibronetciin
Define and explain the physiological function for myoglobin, troponin I and T, natriuretic
peptides (A, B, and C forms), C-reactive protein and homocysteine
Explain the formation, measurement, and clinical significance of modified albumin, and
how it may be utilized in conjunction with troponin and myoglobin results.
During all laboratory and lectures sessions, students are expected to comply with the
General Laboratory Practice/Behavioral objectives provided on the Master Coded
Curriculum Document.
Reading Assignment:
Bishop, M. L., Fody, E. P., & Schoeff, L. E.: Clinical Chemistry: Principles, Techniques, and Correlations,
9th Edition (2022). Chapter 6 Proteins and Heme Derivatives
Additional Materials:
 Power points: Proteins Part 1 & 2, Clinically Significant Proteins, Protein Electrophoresis
Revised 10/10/2023
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