Clinical Chemistry

PROTEINS, LIPIDS and LIPOPROTEINS

PROTEINS

MACROMOLECULES
! Made up of chains of amino acids
! Each amino acid is being linked to another via PEPTIDE BOND
PEPTIDE BOND
 Formed when carboxyl (-COOH) group of one amino acid links to the amino (-NH^2)
group of another amino acid with the loss of water molecule
o N-TERMINAL
end protein structure with a free AMINO group
o C-TERMINAL
End protein structure with a free CARBOXYL group

Protein consists of 16% nitrogen which differentiates proteins from CARBOHYDRATES and LIPIDS.

PROTEIN STRUCTURE

PRIMARY STRUCTURE
! Amino acids are linked to each other through COVALENT PEPTIDE BINDING

SECONDARY STRUCTURE
! Polypeptide chains wind to FORM ALPHA HELIXES and BETA SHEETS
! Through the formation of HYDROGEN BONDS between CO & NH groups of peptide bonds

TERTIARY STRUCTURE
! Coiled polypeptide chain folds upon itself to form 3D STRUCTURE
! Interactions include the formation of disulfide linkages, hydrogen bonds, hydrophobic
interactions and Van der Waals forces

QUARTERNARY STRUCTURE
! Two or more folded polypeptide
! Binds through hydrogen bonds and electrostatic interaction to form a functional protein

CLASSIFICATION OF PROTEINS

SIMPLE PROTEIN
! Polypeptide composed of ONLY AMINO ACIDS
Globular proteins: symmetrical, compactly folded polypeptide chains (albumin)
Fibrous proteins: asymmetrical, elongated polypeptide chains (troponin and collagen)

CONJUGATED PROTEINS
! Composed of protein (apoprotein) and nonprotein (prosthetic group) components:
 Metal, Lipid, and Carbohydrates
 Metalloproteins: protein with metal prosthetic group
 Ceruloplasmin
Lipoproteins: protein with lipid prosthetic group
 Cholesterol, Triglyceride
Glycoproteins: protein with 10-40% carbohydrates attached (haptoglobin)
Mucoproteins: protein with >40% carbohydrase attached (mucin)
Nucleoproteins: protein with DNA or RNA nucleic acids attached (chromatin, chromosomes)

PROTEIN FUNCTIONS
 Energy Production
 Water Distribution
 Acid Base Balance
 Transporter
 Antibodies
 Hormones
 Structural proteins
 Enzymes
 Hemostasis

PLASMA PROTEIN

PREALBUMIN / TRANSTHYRETIN
- Indicator of malnutrition
- Landmark to confirm specimen in CSF
- Transports thyroxine and retinol by binding RETINOL BINDING PROTEIN
- RV: 16-45 mg/dL

 Steroid therapy, Chronic renal failure, Alcoholism

 Liver disorders, Inflammation, Malignancy, Poor Nutrition

ALBUMIN
- Negative APR (Acute Phase Reactants)
- Binds bilirubin, steroids, fatty acids
- Major contributor to oncotic pressure
- ½ plasma protein mass
- Indicator of nutritional status
- Reservoir of amino acids
- RV: 3.5-5.0 g/dL

 Dehydration

 Liver disorders, GIT associated malabsorption, Muscle wasting disease, Severe burns, Renal
Diseases (Nephrotic Syndrome), Glomerulonephritis, Starvation and Malnutrition
ALPHA1 GLOBULINS

A1-ANTITRYPSIN (AAT)
- Acute Phase Reactants
- Protease inhibitor
- 90% of a-1 globulin band
- Inactivates trypsin and other proteolytic enzymes
- RV: 145-270 mg/dL

 Inflammatory response, Estrogen use, Pregnancy

 Hereditary defect (AAT deficiency), Emphysematous pulmonary disease, Juvenile hepatic

cirrhosis

A1-FETOPROTEIN
- Principal fetal protein
- Detectable in maternal blood up to 7th to 8th month of gestation
- Screening done between 15 and 20 weeks gestation
- RV: 5 ng/mL

 Neural tube defects, Spina bifida, Fetal distress, Twins, Hepatoma (>1000 ng/mL), Gonodal
cancer, HDN, Tyrosinosis

 Trisonomy 21, Trisonomy 18