PMID: 6988441Apr 1, 1980Paper

Involvement of an acrosinlike proteinase in the sulfhydryl-induced degradation of rabbit sperm nuclear protamine

The Journal of Cell Biology
B R ZirkinJ Heaps

Abstract

Previous studies demonstrated that proteolytic activity is associated with isolated rabbit sperm nuclei and is responsible for the degradation of nuclear protamine that occurs during thiol-induced in vitro decondensation of the nuclei (Zirkin and Chang, 1977; Chang and Zirkin, 1978). In this study, we present the results of experiments designed to characterize this proteolytic activity. Basic protein isolated from rabbit sperm nuclei incubated with 5 mM dithiothreitol (DTT) and 1 percent Triton X-100 for increasing periods of time exhibited progressively faster migrating bands on acid-urea polyacrylamide gels, reflection the progressive degradation of protamine. Ultimately, a specific and characteristic peptide banding pattern resulted. When sperm nuclei were treated with the esterase inhibitor nitrophenyl-p-guanidino benzoate (NPGB) to inhibit the nuclear-associated proteolytic activity and then incubated with one of several exogenous proteinases in addition to DTT and Triton X-100, characteristic peptide banding patterns were seen for each exogenous proteinase employed. For trypsin, chymotrypsin, pronase, and papain, the peptide banding patterns differed from one another and from the pattern characteristic of protamine degrad...Continue Reading

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Citations

Mar 1, 1982·Developmental Biology·S M Elsevier
Apr 3, 2007·Animal Reproduction Science·T A A KhalifaTh Papanikolaou
Dec 6, 2008·Reproduction in Domestic Animals = Zuchthygiene·A G Lymberopoulos, T A A Khalifa
Oct 1, 1983·The Anatomical Record·D Y Chen, F J Longo
Dec 10, 1982·The Journal of Experimental Zoology·S D Perreault, B R Zirkin
Nov 14, 1983·Biochimica Et Biophysica Acta·T TobitaM Nakano
Mar 1, 1984·Journal of Ultrastructure Research·M Loir, M Lanneau

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