Skip Navigation

This Article
Right arrow FREE Full Text (PDF) Freely available
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 ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (8)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Williams, K.
Right arrow Articles by Hall, L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Williams, K.
Right arrow Articles by Hall, L.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Molecular Human Reproduction, Vol 4, 235-242, Copyright © 1998 by Oxford University Press

JOURNAL ARTICLE

Expression of extracellular superoxide dismutase in the human male reproductive tract, detected using antisera raised against a recombinant protein

K Williams, J Frayne, EA McLaughlin and L Hall
Department of Biochemistry, University of Bristol, School of Medical Sciences, UK.

Mammalian spermatozoa are particularly susceptible to the deleterious effects of reactive oxygen species and lipid peroxidation, which ultimately lead to impaired fertility. A number of enzymes are present in the male reproductive tract which may play a role in preventing oxidative damage; in particular, the epididymis is the site of synthesis and secretion of large amounts of extracellular superoxide dismutase (eSOD). In order to study the distribution of eSOD in the male reproductive tract, and distinguish it from other related superoxide dismutase isoenzymes (e.g. cytosolic SOD), polyclonal antisera have been raised against a recombinant human eSOD fusion protein, expressed in bacterial cells. This protein was expressed from a synthetic gene fragment, using preferred Escherichia coli codons, designed to overcome the problems associated with the high guanine+cytosine content of the natural human eSOD transcript. Using this antiserum, eSOD can be readily detected in a range of human reproductive tissues as well as in human seminal plasma. However, the presence of similar levels of eSOD in the seminal plasma of vasectomized men (probably of prostatic origin) precludes its use as a simple diagnostic indicator of eSOD activity levels in the epididymis.
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Biol. Reprod.Home page
J.-L. Gatti, S. Metayer, M. Belghazi, F. Dacheux, and J.-L. Dacheux
Identification, Proteomic Profiling, and Origin of Ram Epididymal Fluid Exosome-Like Vesicles
Biol Reprod, June 1, 2005; 72(6): 1452 - 1465.
[Abstract] [Full Text] [PDF]

Home page
 Hum ReprodHome page
R.J. Potts, T.M. Jefferies, and L.J. Notarianni
Antioxidant capacity of the epididymis
Hum. Reprod., October 1, 1999; 14(10): 2513 - 2516.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.