Abstract
Chickens were immunized either by a single or by multiple injections of neutral salt-soluble collagen obtained from the skin of lathyritic rats. A distinct antibody activity could be demonstrated to native and denatured collagen by quantitative precipitation and passive hemagglutination. In gel precipitation only denatured collagen and its constituent α-chains reacted. The reaction with the purified polypeptide chains as well as the collagenase susceptibility of such reactions demonstrated that the antibodies are specifically directed to collagen sequences. Collagenase digestion of precipitates allowed the isolation of pure antibodies. They were characterized in immunoelectrophoresis as IgG and IgM, respectively, quite in accordance with results of chromatography on Sephadex G-200. A comparative study with monomeric bovine serum albumin revealed an earlier onset of the antibody response and higher levels of precipitating antibodies in hyperimmune sera.
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