Abstract
Guinea pig antisera to porcine prolactin were characterized by immunodiffusion, quantitative precipitin, and microcomplement fixation techniques. In gel double diffusion tests, the antisera cross-reacted with ovine and bovine prolactins, but not with rat prolactin, porcine growth hormone, or human growth hormone. Microcomplement fixation experiments indicated a considerable degree of immunological similarity among porcine, ovine, and human prolactins. Modification of porcine prolactin either by reduction or oxidation decreased its immunoreactivity and abolished its biological acivity in the pigeon crop-sac assay.
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