| Proteolytic degradation of protamine during thiol-induced nuclear decondensation in rabbit spermatozoa. | |
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MedLine Citation:
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PMID: 641489 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Rabbit sperm nuclei decondensed when incubated with dithiothreitol and Triton X-100. Protamine isolated from these nuclei during the course of treatment exhibited marked and progressive degradation. Timed interval experiments revealed that the degradation of protamine significantly preceded sperm nuclear decondensation and reached its maximum extent before decondensation was completed. Studies with protease inhibitors demonstrated that proteolysis was involved in both nuclear decondensation and protamine degradation. |
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Authors:
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T S Chang; B R Zirkin |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: The Journal of experimental zoology Volume: 204 ISSN: 0022-104X ISO Abbreviation: J. Exp. Zool. Publication Date: 1978 May |
Date Detail:
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Created Date: 1978-06-28 Completed Date: 1978-06-28 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 0375365 Medline TA: J Exp Zool Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 283-9 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Cell Nucleus / drug effects, metabolism Dithiothreitol / pharmacology Male Peptide Hydrolases / pharmacology* Polyethylene Glycols / pharmacology Protamines / metabolism* Rabbits Spermatozoa / cytology, drug effects, metabolism* Sulfhydryl Compounds / pharmacology Time Factors Trypsin Inhibitors / pharmacology |
| Chemical | |
Reg. No./Substance:
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0/Polyethylene Glycols; 0/Protamines; 0/Sulfhydryl Compounds; 0/Trypsin Inhibitors; 3483-12-3/Dithiothreitol; EC 3.4.-/Peptide Hydrolases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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