Biol Reprod Lalor Postdoctoral Fellowships -- Application Deadline January 15, 2009
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow My Folders
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Rousseaux, J.
Right arrow Articles by Rousseaux-Prevost, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Rousseaux, J.
Right arrow Articles by Rousseaux-Prevost, R.
Agricola
Right arrow Articles by Rousseaux, J.
Right arrow Articles by Rousseaux-Prevost, R.

Biology of Reproduction, Vol 52, 1066-1072, Copyright © 1995 by Society for the Study of Reproduction

ARTICLES

Molecular localization of free thiols in human sperm chromatin

J Rousseaux and R Rousseaux-Prevost
Biologie et Pathologie du Spermatozoide Humain, Institut de Recherches sur le Cancer, Lille, France.

The presence in human sperm nuclear proteins of a limited amount of unoxidized thiol groups, stabilized by reversible binding to zinc ions, has been presumed to play a role in the decondensation of sperm within the oocyte. In the present study, the number and molecular localization of free sulfhydryls in the major proteins of human sperm chromatin, protamines P1 and P2, were determined by alkylation of reactive thiols with 14C-iodoacetamide, isolation of protamines, and peptide mapping. Less than 1.5% of the cysteines of protamines were found as reactive thiols, a proportion strikingly lower than that reported previously for whole human sperm proteins. The amount of sulfhydryls was unaffected by the zinc chelating agent EDTA. Labeling was evenly distributed on every cysteine of protamines P1 and P2. The results confirm the extensive stabilization of sperm chromatin by disulfide bridges and show that the unoxidized cysteines remaining at the end of epididymal transit in some protamine molecules may be one of the six (protamine P1) or five (protamine P2) cysteines present in the sequence of each class of protamines. This even distribution of the reactive cysteines could facilitate decondensation of sperm nuclei initiated by a thiol- disulfide exchange.


This article has been cited by other articles:


Home page
 Hum Reprod UpdateHome page
I.M.W. Ebisch, C.M.G. Thomas, W.H.M. Peters, D.D.M. Braat, and R.P.M. Steegers-Theunissen
The importance of folate, zinc and antioxidants in the pathogenesis and prevention of subfertility
Hum. Reprod. Update, March 1, 2007; 13(2): 163 - 174.
[Abstract] [Full Text] [PDF]

Home page
 Hum ReprodHome page
I.M.W. Ebisch, W.H.M. Peters, C.M.G. Thomas, A.M.M. Wetzels, P.G.M. Peer, and R.P.M. Steegers-Theunissen
Homocysteine, glutathione and related thiols affect fertility parameters in the (sub)fertile couple
Hum. Reprod., July 1, 2006; 21(7): 1725 - 1733.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
M. Conrad, S. G. Moreno, F. Sinowatz, F. Ursini, S. Kolle, A. Roveri, M. Brielmeier, W. Wurst, M. Maiorino, and G. W. Bornkamm
The Nuclear Form of Phospholipid Hydroperoxide Glutathione Peroxidase Is a Protein Thiol Peroxidase Contributing to Sperm Chromatin Stability
Mol. Cell. Biol., September 1, 2005; 25(17): 7637 - 7644.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1995 by the Society for the Study of Reproduction.