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IMMUNOGLOBULIN STRUCTURE AND FUNCTION. September 20, 2006. THE TWO FORMS OF ANTIBODY. Membrane form is on the surface of B cells. Plasma cells make the secreted form which is found plasma, lymph, and interstitial fluid. The secreted form can also be found on the surface of cells with FcR.
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IMMUNOGLOBULIN STRUCTURE AND FUNCTION September 20, 2006
THE TWO FORMS OF ANTIBODY Membrane form is on the surface of B cells Plasma cells make the secreted form which is found plasma, lymph, and interstitial fluid. The secreted form can also be found on the surface of cells with FcR
IMMUNOGLOBULINS HAVE 4 POLYPEPTIDE CHAINS 2 Identical H(eavy) chains 2 Identical L(ight) chains
ANTIBODY MOLECULES HAVE GLOBULAR REGIONS The globular regions are separated by a hinge region The globular regions contain globular domains
THE STRUCTURE OF THE DOMAINS PROVIDES STABILITY Domains are approximately 110 amino acids Amino acids are aligned in b sheets V and C are slightly different
ANTIBODY MOLECULES CAN BE CLEAVED BY PROTEOLYTIC ENZYMES Cleavage separates functionally distinct parts of protein
Figure 3-4 HINGE REGION PROVIDES FLEXIBILITY Electron micrographs of ag-ab interaction demonstrates flexibility
AN ANTIBODY BINDS AN EPITOPE OF THE ANTIGEN Antibody molecule binds epitopes on a viral particle
Figure 3-8 Antigen Binding Site Can Have Different Shapes 4 types: pocket, groove, extended surface and protruding surface
THE DIFFERENT CLASSES OF ANTIBODY There are two types of L chain: k and l There are 5 types of H chain: g, m, d, a, e A complete antibody molecule has 2 identical light chains and 2 identical heavy chains
Ig Can Block Adherence of Bacteria IgA at mucosal surfaces IgG at other sites
OPSONIZATION (IgG and IgA) Opsonization requires matching between FcR and Ig
ADCC(IgG) ADCC also requires FcR and Ig isotype matching