Albumin and its Biochemical Functions

This text discusses albumin, a major protein found in blood plasma. Here's a breakdown of the
key information:

Albumin Properties:
 Function: Makes up 58% of plasma proteins.
 Source: Synthesized by liver (hepatocytes).
 Structure: Single polypeptide chain with 585 amino acids, 17 disulfide bonds.
 Molecular weight: 69,000 Daltons.
 Type: Simple globular protein.
 Isoelectric pH: Around 4.7.
 Solubility: Precipitated by ammonium sulfate.
 Half-life: About 20 days.
 Production rate: 10-15 grams per day by the liver (25% of total hepatic protein synthesis).
 Location: Blood plasma, cerebrospinal fluid (CSF), interstitial fluid.

Biochemical Functions:
1. Maintenance of Colloidal Osmotic Pressure:
o Contributes 60-80% of total plasma osmotic pressure (25 mmHg).
o Plays a vital role in maintaining blood volume and body fluid distribution.
o Low albumin levels lead to decreased osmotic pressure and fluid retention in tissues (edema) -
occurs when albumin falls below 2 grams per deciliter (hypoalbuminemia).
o Explained by Starling hypothesis:
 Arterial end: Hydrostatic pressure (outward) = 35 mmHg, Osmotic pressure (inward) = 25
mmHg -> Net outward force = 10 mmHg.
 Venous end: Hydrostatic pressure (inward) = 15 mmHg, Osmotic pressure (inward) = 25 mmHg
-> Net inward force = 10 mmHg.
 Low albumin disrupts this balance, leading to fluid accumulation in tissues.

2. Transport Function:
 Albumin binds and transports various biochemically important compounds poorly soluble in
water through the bloodstream.
 Examples include:
o Free fatty acids
o Bilirubin
o Steroid hormones
o Calcium and copper ions
o Drugs (sulfonamides, penicillin, dicoumarol, aspirin, digoxin)
3. Nutritive Function:
 Albumin is a complete protein, providing essential amino acids during malnutrition.
 During limited protein intake, albumin breakdown supplies amino acids for tissue protein
synthesis.
 It acts as a transport form of essential amino acids from the liver to other body cells.
4. Buffering Function:
 Albumin has the highest buffering capacity among plasma proteins due to its 16 histidine
residues.
 However, the bicarbonate buffer system plays a more significant role in blood pH regulation.

Clinical Significance:
 Normal Albumin Level: 3.5 to 5 grams per deciliter
 Measurement Method: Bromocresol green (BCG) method
 Sample Collection: Green or red vacutainer tube

Clinical Significance - Hypoalbuminemia:

 Defined as serum albumin level below 2 grams per deciliter.
 Causes (pathological):
o Reduced Synthesis:
 Chronic liver disease (cirrhosis)
 Severe protein-energy malnutrition
 Intestinal malabsorption diseases
 Abnormal Distribution:
 Increased capillary permeability (severe burns, edema, ascites) - plasma leaks into extravascular
space.
o Abnormal/Excessive Losses:
 Nephrotic syndrome (damaged glomerular membrane) - albumin loss in urine (high
albuminuria).
 Gastrointestinal diseases (protein-losing enteropathy)
 Burns, skin diseases
 Hemorrhage, inflammation
 Hemodilution (loss of protein into extravascular space)
o Increased Catabolism:
 Infection, trauma, burns (increased protein breakdown)
o Overhydration:
 Excessive fluid intake dilutes albumin concentration (less significant)
 Increased Catabolism:
o Injury (major surgery, trauma)
o Infection
o Fever
o Malignant disease (increased protein breakdown)
 Overhydration:
o Excessive fluid intake dilutes albumin concentration (less significant)

Hyperalbuminemia (Increased Albumin Levels):

 Rare condition with no clinical significance.
 Can occur in acute dehydration.

Analbuminemia (Hereditary Albumin Deficiency):

 Autosomal recessive genetic disorder.

 Plasma albumin concentration is less than 1 gram per deciliter, or absent entirely.
 Albumin levels range from 0.1 to 1 gram per deciliter.
 May have no symptoms or edema due to increased globulin levels to compensate.

Albumin and Blood-Brain Barrier:

 Albumin-fatty acid complexes cannot cross the blood-brain barrier, preventing liver uptake of
fatty acids.
 Drugs like aspirin can compete with bilirubin for albumin binding sites, allowing free
(unconjugated) bilirubin to cross the blood-brain barrier.
 In young children, free bilirubin deposition in the brain can lead to kernicterus (a form of
encephalopathy) and mental retardation.

Albumin and Drug Interactions:

 Competition between drugs with high albumin binding affinity can increase the free fraction of
one drug, affecting its potency.
 Example: Phenytoin and dicoumarol interaction.

Protein-Bound Calcium:
 Low albumin levels (hypoalbuminemia) decrease total blood calcium levels.
 However, ionized calcium (active form) may remain normal, preventing tetany (muscle cramps).
 Every 0.8 mg/dL decrease in calcium corresponds to a 1 g/dL decrease in albumin.

Multiple Choice Questions: Albumin

1. Albumin Synthesis
 A. Liver (Correct)
 B. Kidney
 C. Spleen
 D. Skeletal Muscle
2. Albumin Functions
 A. Maintains colloidal osmotic pressure
 B. Plays a role in body immune response (Incorrect)
 C. Serves as a transporter
 D. Acts as a buffer
 E. All of the above (Except B) (Correct)
3. Albumin Transport
 A. Bilirubin
 B. Free fatty acids
 C. Thyroxine
 D. Iron (Incorrect)
 E. All of the above (Except D) (Correct)
4. Albumin Use in Treatment
 A. Burns
 B. Hemorrhage
 C. Severe liver disease
 D. All of the above (Correct)