Abstract
Changes in nuclear basic proteins throughout ram spermiogenesis were analysed by electrophoresis on polyacrylamide gels. Four spermatid populations were obtained by sedimentation at 1 gravity. Acid-soluble proteins were extracted from nuclei prepared with 0.05% Triton X-100. Somatic histones present in round spermatid nuclei are displaced from chromatin while nuclei elongate and condense. They are replaced by a unique basic protein, acid-soluble in the first stage of its synthesis, then acid-insoluble unless treated with 2-mercaptoethanol. Several basic proteins faster or slightly slower than F2a1 are present in nuclei involved in this process of replacement.
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