Boar malpha-acrosin. Purification and characterization of the inital active enzyme resulting from the conversion of boar proacrosin to acrosin.
نویسندگان
چکیده
منابع مشابه
Proacrosin conversion inhibitor. Purification and initial characterization of a boar sperm protein which prevents the conversion of proacrosin into acrosin.
A proacrosin conversion inhibitor present in boar spermatozoa has been purified and initially characterized. Purification methods included sequential acid extractions of washed spermatozoa at pH 4.0, pH 3.5, and pH 2.5 followed by successive gel filtrations of the pH 2.5 sperm extract supernatant over Sephadex G-75 and G-50. The resulting 8.8-fold purified materials were judged to be homogeneou...
متن کاملBoar acrosin. I. Purification and preliminary characterization of a proteinase from boar sperm acrosomes.
Acrosin is a proteolytic enzyme used by sperm to digest a path through the zona pellucida of the ovum. In ejaculated sperm it is inactivated by a proteinase inhibitor from seminal plasma that also inhibits trypsin. This inhibitor is removed or inactivated during the residence in the female reproductive tract as a part of the capacitation process. The boar acrosin-inhibitor complex was partially...
متن کاملExpression and tyrosine phosphorylation of sp32 regulate the activation of the boar proacrosin/acrosin system.
The current study investigated the relationship between the level of expression and tyrosine phosphorylation of the sperm protein 32 (sp32) and the activation of the boar proacrosin/acrosin system. The acrosomal membrane proteins of boar sperm for use in different treatment experiments (i.e., fresh sperm, freezing and thawing, capacitation, and acrosome reaction) were separated, stained by Coom...
متن کاملBoar proacrosin. Purification and preliminary activation studies of proacrosin isolated from ejaculated boar sperm.
Two forms of proacrosin have been purified from ejacualted boar spermatozoa. The isolation method utilized benzamidine to inhibit the premeture activation of the zymogen and included pH precipitation, ammonium sulfate fractionation, and sodium chloride precipitation. Further purification was achieved by Sephadex G-200 FILTRATION OF THE PREPARATION AFTER IT WAS TREATED WITH 8 M urea. The overall...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1978
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)34309-0