SEQUENCE HOMOLOGIES OF AN ANDROGEN-REGULATED PROTEIN SECRETED BY THE MOUSE CAPUT EPIDIDYMIDIS WITH GLUTATHIONE PEROXIDASES

被引：0

作者：

GHYSELINCK, NB ^{[1
]}

RIGAUDIERE, N ^{[1
]}

DUFAURE, JP ^{[1
]}

机构：

[1] CNRS,URA 360,F-63170 CLERMONT FERRAND,FRANCE

来源：

COMPTES RENDUS DE L ACADEMIE DES SCIENCES SERIE III-SCIENCES DE LA VIE-LIFE SCIENCES | 1991年 / 313卷 / 01期

关键词：

LIPID-PEROXIDATION; HYDROGEN-PEROXIDE; SPERMATOZOA; SPERM; SELENOCYSTEINE; SUPEROXIDE; MOTILITY; CDNA; SITE;

D O I：

暂无

中图分类号：

Q [生物科学];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Principal cells of the mouse caput epididymidis synthesize and secrete a 24 kDa protein able to bind to the head of the spermatozoa. Sequencing of several clones selected from cDNA and genomic libraries, combined with the microsequencing of the NH2 terminus of the protein allowed to reconstitute the entire primary structure of the mature 24 kDa protein. It revealed 81% homology with a human plasma glutathione peroxidase and 61% homology with a mouse erythrocyte glutathione peroxidase. This enzyme, once secreted in the epididymal fluid, might protect sperm membrane lipids, particularly those of the acrosomal part, against peroxidation.

引用

页码：1 / 6

页数：6

共 22 条

[1] MOVEMENT CHARACTERISTICS OF BOVINE EPIDIDYMAL SPERMATOZOA - EFFECTS OF FORWARD MOTILITY PROTEIN AND EPIDIDYMAL MATURATION [J].