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- The elucidation of antibody structure The introduction of the technique of ion-exchange CHROMATOGRAPHY in the 1950s allowed rabbit IgG, the most abundant class of immunoglobulin in immunized animals, to be purified from serum in a single step. As specific antibody responses were also readily induced in rabbits, this laboratory animal was used in many of the early definitive investigations. Studies of the pattern of protein fragmentation following digestion of antibody with the enzyme papain, by Rodney Porter, and of the polypeptide chain components, by Gerry Edelman, led Porter to propose the four-chain structure for rabbit IgG in 1959 (see Fig. A40). This model proposed that each individual IgG molecule is composed of two light chains of Mr 25,000, of identical amino-acid sequence, and two heavy chains of Mr 50,000 also of identical amino-acid sequence. The light chains are covalently bound to the heavy chains through a single disulphide bridge and the heavy chains are similarly covalently linked to each other through one or more disulphide bridges (the number of disulphide bridges between heavy chains varies with isotype and species). Reduction of the disulphide bridges does not result in dissociation of the molecule, under physiological conditions, owing to the presence of multiple light-heavy and heavy-heavy interchain noncovalent bonds.
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