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The perforatorium of rat spermatozoa was isolated and its protein composition determined. SDS-polyacrylamide gel electrophoresis showed that the organelle is composed of a single polypeptide component with a molecular weight of 13,000. The perforatorium becomes more resistant to solubilization during epididymal transit due to an apparent increase in disulphide bond content. Amino acid analysis of the perforatorium polypeptide revealed a content of 6-5% cysteine.
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Olson et al. (1976) studied this question.
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