Document Detail


Proteolytic degradation of protamine during thiol-induced nuclear decondensation in rabbit spermatozoa.
MedLine Citation:
PMID:  641489     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
T S Chang; B R Zirkin
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of experimental zoology     Volume:  204     ISSN:  0022-104X     ISO Abbreviation:  J. Exp. Zool.     Publication Date:  1978 May 
Date Detail:
Created Date:  1978-06-28     Completed Date:  1978-06-28     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0375365     Medline TA:  J Exp Zool     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  283-9     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
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:
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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