The document summarizes plasma proteins and immunoglobulins. It states that total plasma proteins are 6-8 g/dl, consisting mainly of albumin, globulins, and fibrinogen. Albumin and fibrinogen are synthesized solely by the liver, while globulins are produced in both the liver and lymphoid tissues. Immunoglobulins constitute approximately 20% of plasma proteins and are produced by plasma cells and lymphocytes in response to antigens. The five main classes of immunoglobulins are IgG, IgA, IgM, IgD, and IgE, which have different structures and functions.

1. PLASMA PROTEINS

3. • Total proteins of plasma is 6-8 g/dl.
1) Albumin : 3.5 – 5 g/dl
2) Globulins:2.5-3.5 g/dl and
3) Fibrinogen:0.2 - 0 .4 g/dl

4. Synthesis of Plasma Proteins
▪ All the albumin and fibrinogen are synthesized by the
liver onl
▪ Similarly 50 to 80% of the globulin is formed in the liver
▪ The remainder of the globulins are formed almost
entirely in the lymphoid tissues.
▪ The A/G ratio can be altered in the liver disease.

5. Separation of plasma proteins
1. Salting out
2. Cohn's fractionation and
3. Electrophoresis

6. Electrophoresis

7. Functions of plasma proteins
• Transport function
• Nutritive function
• Buffering action
• Colloidal osmotic pressure
• Antiproteases
• Blood coagulation
• Hormones
• Immunity
• Involvement in inflammatory responses

8. ALBUMIN
• Albumin is a globular protein with 585 amino acid residues
accounting for approximately 50% of plasma protein
• Albumin is synthesized exclusively by the liver.
Functions of albumins
Albumin plays a predominant role in:
▪ Maintenance of colloid osmotic pressure of plasma.

11. ▪ Transport of metabolites which are poorly soluble in
water :
▪ Fatty acids
▪ Bilirubin
▪ Calcium
▪ Certain steroid hormones
▪ Copper
▪ Some of the plasma tryptophan
▪ A variety of drugs, like sulfonamides, penicillin
G, dicumarol, aspirin, and digoxin

12. • Buffering function: albumin has maximum buffering
capacity
• Nutritive function : Degradation of albumin provide
essential amino acids during malnutrition.

13. Clinical significance
Hypoalbuminaemia: Malnutrition, nephrotic syndrome, cirrhosis of
liver
Hyperalbuminaemia: Acute dehydration have no clinical significance.
Analbuminaemia (less than 1gm/l , normal= 3.5 to 6gm/dl):
Analbuminaemia is a rare hereditary abnormalities there may be no
symptoms or signs not even edema due to compensatory increase in
plasma globulin concentration.

14. Acute phase proteins
• The level of these proteins increases within 1-
5 days after an inflammation , trauma or
surgery.
• Examples :CRP,apha1-
antitrypsin,haptoglobin,ceruloplasmin etc.

15. Immunoglobulins (Ig)
• The immunoglobulins are γ -globulins, called
antibodies.
• Constitute about 20% of all the plasma proteins
• produced by plasma cells and by lymphocytes in
response to a variety of antigen.

16. Schematic structure of immunoglobulin G.

17. ▪ The basic immunoglobulin is Y shaped consist of four
polypeptide chains:
– two H and
– two L chains
▪ The four chains are linked by disulfide bond
▪ L chain may be either of two types, Kappa (қ) or
Lambda (λ) but not both

18. ▪ The heavy chains may be of five types and are
designated by Greek letter:
– alpha (α)
– gamma (γ),
– delta (δ),
– mu (μ) and
– epsilon (ε)
▪ Immunoglobulins are named as per their heavy chain
type as IgA, IgG, IgD, IgM and IgE

19. ▪ The L and H chains are subdivided into variable ( towards
the carboxyl terminal end) and constant ( towards the
amino terminal end) regions.
▪ L chain consists of one variable (VL) and one constant
(CL) domain or region.
▪ Most H-chains consist of one variable (VH) and three
constant (CH-1, CH-2, and CH-3) domains.

20. ▪ The hinge region between the CH-1 and CH-2 domains
confers flexibility and allows both Fab arms to move
independently , thus helping them to bind to antigenic site

21. Light chain type
• Light chain may be either of two types, Kappa (k) or
Lambda (l) but not both.
• In a given immunoglobulin either 2k or 2 l but not the
mixture of kappa and lambda
• Most abundant light chain in human is k

22. ▪ Enzyme (papain) digestion splits the
immunoglobulin molecule into two fragments
1. Fab: Fragment for antigen binding. Located in
variable region.
2. Fc: Crystallisable fragment or fragment for
complement binding

23. Monomeric, dimeric, and pentameric forms of
immunoglobulins.

26. Classes of immuoglobulins
1. IgG
2. IgA
3. IgM
4. IgD
5. IgE

27. IgG
• It constitutes 75-80% of total
immunoglobulins
• Major antibody in secondary immune
response
• Subclasses of IgG
• Crosses the placenta
• Opsonises bacteria

28. IgA
• Second most abundant Ig
• Present in body secretions like colostrum,
saliva,tears , respiratory ,intestinal and genital
tract secretions.
• It prevents attachment of microorganisms to
mucous surfaces.
• It occurs as a monomer or dimer joined by a j
chain.

29. IgM
• Pentamer
• First antibody produced when an antigen
enters organism.
• It is most efficient Ig in agglutination
complement activation.

30. IgD
• It’s a monomer
• Present in very low concentration
• Present on the surface of B lymphocytes.
• Exact function is not known.

31. IgE
• Monomer
• It mediates allergic reactions , hypersensitivity
and anaphylaxis.
• It stimulates the mast cells to release
histamine.