Structure, types and functions of Antibody.PPT
- 1. Antibody
- 2. Antibody is a protective protein produced by immune system in response to the presence of antigen. It is plasma protein produced by B lymphocytes. Chemically it is glycoprotein in nature. It have property of combining with specific antigens. ANTIBODY
- 3. Serum proteins Albumins Globulins Alpha 1 globulins Alpha 2 globulins Beta globulins Gamma globulins IMMUNOGLOBULIN
- 4. Structure of Antibody Light chain: 214 amino acids 25,000d Kappa (k) & Lambda (λ) Heavy chain: 50,000d α, β, µ, Ү, ԁ
- 10. Types of antibodies Based on structural differences and biological properties types of antibodies are: 1. Ig G 2. Ig A 3. Ig M 4. Ig D 5. Ig E
- 11. Immunoglobulin G It is a typical antibody consisting 2 heavy chains and 2 light chains. Accounts for 70% of total immunoglobulin in human serum. It’s concentration in normal serum is about 8-26 mg/litre. Produced during secondary immune response. Molecular weight: 1,50,000 d. Sedimentation coefficient is ‘7’s. Carbohydrate content is 3%. There are four antigenically distinct subclasses of IgG as IgG1, IgG2, IgG3, IgG4 and IgG5.
- 12. Biological Functions of IgG 1. It is only immunoglobulin that crosses the human placenta. Thus it gives protection to newborn for about 6-9 months. 2. It activates classical complement pathway during Ag-Ab reactions. 3. It neutralizes toxins and viruses. 4. Works as opsonins during phagocytosis.
- 13. Immunoglobulin M (IgM) It is largest immunoglobulin. Molecular weight: 9,50,000 d (Macroglobulin). It is pentameric, each with four polypeptide chain.
- 14. Concentration in serum is about 2-5 mg/ml. Half life period: 5 days Carbohydrate content: 10-12%. Sedimentation coefficient: 19s No subclasses of IgG. It is earliest immunoglobulin to be synthesized by foetus. The number of antigen binding sites on IgM are only 5. However, human and rabbit IgM contains 10 sites.
- 15. Biological Functions of IgM 1. It is the first antibody to appear in primary immune response but have short half life period. So it is used as indicator of recent infection. 2. Human foetus can synthesize IgM antibodies, if it’s B cell are antigenically stimulated. 3. It has high functional affinity for multivalent antigens. e.g. It can react with polyvalent antigens as RBC’s or E. coli cells. 4. Also shows properties such as opsonization, complement fixation, agglutination etc.
- 16. 5. Because of its macromolecule size, it is located in blood and thus gives protection against blood infections. 6. ABO blood group antigens are of Ig M type.
- 17. Immunoglobulin A (IgA) IgA is found only to some extent in blood serum, but predominantly in tears, saliva, colostrum and in secretions of respiratory, gastrointestinal and urinogenital tracts. Hence also known as secretory antibodies. Second in abundance i.e. 10-15%. There are two subclasses of IgA as IgA1 and IgA2. Serum IgA is a monomer having structure similar to IgG. Molecular weight: 1,60,000d. But human secretary IgA is dimer linked by ‘J’ chain with mol.wt. 5,00,000d.
- 18. IgA is synthesized by plasma cells in lamina propria of mucous membrane. Carbohydrate content: 10% Sedimentation coefficient: 7s Serum concentration: 0.6 to 4.2 mg/litre. Half life period: 6-8 days. Have 2 subclasses as IgA1 and IgA2.
- 19. Biological functions of IgA 1. Secretary IgA is termed as mucosal paint or antiseptic paint of mucosal membrane. 2. Neutralizes toxins and promotes phagocytosis. 3. Found to produce immunity against tapeworms. 4. IGA is present in colostrum and thus protect the baby from intestinal pathogens.
- 20. Immunoglobulin D (IgD) Has typical antibody structure with 4 polypeptide chains. It is slightly larger than Ig G with mol.wt. 1,80,000d. Serum concentration: 0.03 mg/litre. Sedimentation coefficient: 7s Carbohydrate: 12% Rate of synthesis is 0.4 mg/Kg body weight/ day. Half life is 2-3 days. There are 2 subclasses of IgD as IgD1 and IgD2.
- 21. Biological functions of IgD 1. IgD has not been shown to have antibody activity. So no direct role in the specific defence mechanism. 2. Acts as a receptors for antigens on the surfac of B lymphocytes.
- 22. Immunoglobulin E (IgE) It is a monomer with typical immunoglobulin structure. Molecular weight: 1,90,000d. It is heat labile immunoglobulin. It is found only in trace amount in serum, average serum level is 0.00004 mg/litre. But in persons with allergic conditions, it’s level may be 50-100 times higher. Half life period: 2-3 days. Sedimentation coefficient: ‘8’ s
- 23. It has binding affinity for mast cells and basophilrs, which posses receptors for Fc region of IgE. Carbohydrate content: 12% It is usually known as ‘skin sensitizing antibody’. It is also known a “reagin antibody”, as it is significant in allergic reactions.
- 24. Biological functions of Ig E 1. Protective role in childrens with parasitic infections in intestine. 2. IgE mediates reaginic hypernsitivity (Type I hypersensitivity).
- 25. Antibodies can also be categorized on the basis of their functions: 1. Agglutinins:
- 26. 2. Precipitins: They combine with soluble antigens like tetanus toxins and this complex becomes insoluble, gets precipitated and toxin is inactivated. 3. lysins: Some antibodies can bind to cellular agents and causes their lysis. 4. Antitoxins: Antibodies that neutralize the toxins of organisms.
- 27. 5. Opsonins: 6. Complement fixing antibodies: