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                                       Details for article 17 of 32 found articles
 
 
  PHGPx and spermatogenesis
 
 
Title: PHGPx and spermatogenesis
Author: Antonella Roveri
Fulvio Ursini
Leopold Flohé
Matilde Maiorino
Appeared in: BioFactors
Paging: Volume 14 (2001) nr. 1-4 pages 213-222
Year: 2001-08-17
Contents: PHGPx of rat sperm mitochondrial capsule is cross-linked and inactive. The enzyme is in part released in an active form by mercaptoethanol. Treatment with H_2O_2 of reduced and solubilised capsule proteins, in the absence of any added reductant, results in: i) H_2O_2 consumption which depends on the presence of both, PHGPx activity and protein thiols; ii) protein thiol oxidation with a stoichiometry of 2 equivalents of thiol per mole of hydroperoxide and, iii) PHGPx inactivation and cross-linking. SDS-PAGE analysis of monobromobimane-labeled proteins, following incubation with H_2O_2, shows that the oxidation takes place in specific bands in the area of 20~kDa. It is concluded that the protein thiol peroxidase activity of PHGPx is responsible for cross-linking proteins in the mammalian sperm capsule and accounts for the selenium dependency of spermatogenesis.
Publisher: IOS Press
Source file: Elektronische Wetenschappelijke Tijdschriften
 
 

                             Details for article 17 of 32 found articles
 
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