Isolation and characterization of the perforatorium of rat spermatozoa

Abstract
The perforatorium of rat spermatozoa was isolated and its protein composition determined. SDS-polyacrylamide gel electrophoresis showed that the organelle was composed of a single polypeptide component with a MW of 13,000. The perforatorium was more resistant to solubilization during epididymal transit due to an apparent increase in disulfide bond content. Amino acid analysis of the perforatorium polypeptide revealed a content of 6.5% cysteine.

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