Structural and Antigenic Relationships Between Avian Immunoglobulins

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Abstract
Ring-necked pheasants produced IgM hemagglutinating antibodies 3 days following a single injection of bovine serum albumin (BSA). Seven days following injection, IgG and IgM anti-BSA antibodies were detected by the method of radioimmunoelectrophoresis. Compared to chickens and pheasants, Japanese quail respond very poorly to injections of BSA. Chicken IgG (C-IgG), pheasant IgG (P-IgG) and quail IgG (Q-IgG) were similar in several respects: their sedimentation coefficients, which ranged from 7.1S to 7.3S; their yields of heavy (H) and light (L) chains from reduced and acid-dissociated molecules; and the patterns formed by H- and L-chains in urea starch gel electrophoresis. The most striking similarity between the IgGs of these avian species was that, unlike mammalian IgG, partial dissociation of the molecules occurred following reduction in the absence of a dispersing agent. In alkaline buffer, C-IgG and P-IgG each required 0.05 to 0.1 M 2-mercaptoethanol (ME) for release of L-chains, whereas Q-IgG required 0.2 M ME. About 35% of the C-IgG, P-IgG and Q-IgG each dissociated in the absence of a dissociating agent when reduced with 0.2 M ME. As with chicken IgM, reduction of pheasant IgM caused the release of some L-chains.

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