Searching across hundreds of databases

Our searching services are busy right now. Your search will reload in five seconds.

X
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

X
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

Dual function of the selenoprotein PHGPx during sperm maturation.

Science (New York, N.Y.) | Aug 27, 1999

The selenoprotein phospholipid hydroperoxide glutathione peroxidase (PHGPx) changes its physical characteristics and biological functions during sperm maturation. PHGPx exists as a soluble peroxidase in spermatids but persists in mature spermatozoa as an enzymatically inactive, oxidatively cross-linked, insoluble protein. In the midpiece of mature spermatozoa, PHGPx protein represents at least 50 percent of the capsule material that embeds the helix of mitochondria. The role of PHGPx as a structural protein may explain the mechanical instability of the mitochondrial midpiece that is observed in selenium deficiency.

Pubmed ID: 10464096 RIS Download

Mesh terms: Animals | Electrophoresis, Gel, Two-Dimensional | Electrophoresis, Polyacrylamide Gel | Glutathione Peroxidase | Infertility, Male | Male | Mitochondria | Oxidation-Reduction | Proteins | Rats | Rats, Wistar | Selenium | Selenoproteins | Solubility | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | Spermatids | Spermatogenesis | Spermatozoa

Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.

We have not found any resources mentioned in this publication.