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    Immunoglobulins Class

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    Koushali Banerjee
    Immunoglobulins are antibody molecules that are globular proteins found in blood serum that are synthesized in response to antigens. They have a basic Y-shaped structure composed of heavy and light chains that gives them antigen binding and effector functions. The main classes of immunoglobulins are IgG, IgA, IgM, IgD, and IgE which have different structures, functions, and roles in immunity.

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    Immunoglobulins Class

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    Koushali Banerjee
    366 views16 pages
    Immunoglobulins are antibody molecules that are globular proteins found in blood serum that are synthesized in response to antigens. They have a basic Y-shaped structure composed of heavy and light chains that gives them antigen binding and effector functions. The main classes of immunoglobulins are IgG, IgA, IgM, IgD, and IgE which have different structures, functions, and roles in immunity.

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    Immunoglobulins are antibody molecules that are globular proteins found in blood serum that are synthesized in response to antigens. They have a basic Y-shaped structure composed of heavy and light chains that gives them antigen binding and effector functions. The main classes of immunoglobulins are IgG, IgA, IgM, IgD, and IgE which have different structures, functions, and roles in immunity.

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    Attribution Non-Commercial (BY-NC)
    Download as PPTX, PDF, TXT or read online from Scribd
    Download as pptx, pdf, or txt
    366 views16 pages

    Immunoglobulins Class

    Uploaded by

    Koushali Banerjee
    Immunoglobulins are antibody molecules that are globular proteins found in blood serum that are synthesized in response to antigens. They have a basic Y-shaped structure composed of heavy and light chains that gives them antigen binding and effector functions. The main classes of immunoglobulins are IgG, IgA, IgM, IgD, and IgE which have different structures, functions, and roles in immunity.

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    Immunoglobulins/ Antibodies

    Antibody molecules are globular proteins with immune function. Found in the serum fraction of blood. Antibodies are synthesized in response to a antigenic stimulus by a sub population of WBC in immune system called Lymphocytes.

    Functions: Antigen binding Participation in effector functions depending on the physical properties of the antibodies.

    Basic structure of Ig is same. Can be separated by cleavage of molecule with a proteolytic enzyme - Papain. Papain splits the Ab into two identical Fc fragments (Crystallisable fragment) Every monomeric Ab has 2 pairs of polypeptide linked to each other by disulfide bonds. Larger pair 2 heavy chains mol wt- 50000 da each Joined by 1-5 s-s bonds depending on the class of Ig Smaller pair 2 light chains mol wt 25000 da each. L chain attached to H by a s-s bond.

    Antibody Structure
    Ig domain: 110 amino acids; globular domain used in many proteins. Variable domains, Constant domains, Hinge. Fab: fragment antigen binding Fc: fragment crystallizable (effector functions)

    New Science Press Ltd. 2003

    The H chain are structurally and antigenically distinct for each class and are designated by the greek letter corresponding to the Ig class:
    Ig class/ isotopes Ig G Ig A Ig M Ig D Ig E Designation of H-chain (Gamma) (alpha) (Mu) (Delta) (Epsilon)

    Antibody Classes: Structure

    New Science Press Ltd. 2003

    The L chain occurs in two varieties: Kappa (K) and Lambda () Ig may either have K or but not both. The L and H chains of Fab region shows two regions: Constant region: amino acid sequence relatively constant. Variable region: variable amino acid sequence. These regions VL and VH are responsible for formation of a specific Ag binding site.

    Types of immunoglobulins
    Human sera contains the antibodies in the order of descending concentrations: Ig G Ig A Ig M Ig D Ig E

    Immunoglobulin G
    Most common Antibody in human serum 75% of Ab in serum Mol wt 150,000 da Only Ig that passes from mother to foetus major source of passive immunity. Ig G binds to microbes and enhances phagocytosis with most Ag Ig G is a late Ab, appears after initial IR Ig G participates in most immunological reactions. 4 sub classes - IgG1, IgG2, IgG3 and IgG4 each with distinct chain.

    Immunoglobulin A
    2nd most abundant Ig 10% of human sera Mol wt 160,000 da Exists as a dimer, units joined by J chain (joining chain) Occurs in mucous, semen, saliva, tears, sweat. Plays a important role in GI and GU tract. Secreted into human breast milk, plays important role in protecting new borns against infectious diseases. Ig A binds to surface of M.O prevents adherence of such coated microbes to mucosal cells and kills the m.o. Two subclasses : IgA1, IgA2A

    Immunoglobulin M
    Largest Ig Mol wt 900,000 da Exists as a pentamer (5 monomers) held by s-s bonds and a ring J protein. 1st Ab to be produced in a primary immune system. IgM effective in attaching to multiple cells with same surface Ag because of its high number of Ag binding sites. IgM with Ig G are important in preventing the circulation of m.os through the circulatory system. IgM are relatively short lived. Single molecule of IgM can bring about immune haemolysis, 1000 Ig G molecules are required for the same effect.

    Immunoglobulin D
    Mol wt 180,000 da Present on surface of some lymphocyte cells together with IgM. Acts as primary receptor for specific Ag on surface of foetal lymphocytes that are destined to become Ab forming cells in adult life within blood plasma. Short lived Susceptible to enzymatic degradation.

    Immunoglobulin E
    Mol wt 190,000 da Very low proportion in blood serum. Responsible for hypersensitivity or allergic reactions. It is homocytotropic ab, can bind to Ig E specific Fc receptors on membranes of blood basophils and mast cells of own tissues. When Ag like a pollen allergin or a parasite combines with IgE on mast cells, cytoplasmic basophilic granules are activated releasing chemical mediators.(histamines and serotoxins) These mediators in the respiatory tract cause allergy symptoms. These Ags cause a typical wheal and flare rxn. In sensitive individuals. Release of histamines may result in destruction of parasites.

    Functional names of Antibodies


    Abs are designated by names that describe their rxns in vitro or in vivo, when allowed to act upon by certain types of Ag. Antitoxins- neutralise toxins Agglutins cause clumping of bacterial cells for which they are specific. Precepitins cause precipitation or flocculation of extracts of bacterial cells or other soluble Ags Lysins cause lysis Opsonins render microbes more susceptible to ingestion by phagocytosis.

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