Novel seminal phospholipase A(2) is inhibited by the major proteins of bovine seminal plasma

被引：17

作者：

Soubeyrand, S

Manjunath, P

机构：

[1] UNIV MONTREAL,DEPT MED,MONTREAL,PQ H3C 3J7,CANADA

[2] UNIV MONTREAL,DEPT BIOCHEM,MONTREAL,PQ H3C 3J7,CANADA

[3] HOP MAISON NEUVE ROSEMONT,GUY BERNIER RES CTR,MONTREAL,PQ H1T 2M4,CANADA

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 1997年 / 1341卷 / 02期

基金：

加拿大自然科学与工程研究理事会;

关键词：

bovine seminal plasma; BSP protein; phospholipase A(2); phospholipase A(2) inhibition; lipid-binding protein; sperm maturation;

D O I：

10.1016/S0167-4838(97)00070-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The activity of a novel phospholipase A(2), isolated from bovine seminal plasma, was completely inhibited by low concentrations of the major proteins of bovine seminal plasma (BSP proteins). The inhibition was observed towards micellar as well as liposomal phosphatidylcholine. By solid phase binding assay it was determined that the inhibition involved a reduced accessibility to the lipidic substrate. Since the HSP proteins interact with choline phospholipids and since this interaction can be prevented by low concentrations of free choline, the effect of choline on the inhibition was studied. Choline could only partially relieve, even at high concentrations, the phospholipase A(2) inhibition. The reduced accessibility appears to proceed via two distinct interactions: binding to the substrate on one hand and to the enzyme on the other hand. These results indicate that the BSP proteins may act as spermatozoa stabilizing agents by preventing premature lipolysis of the sperm surface. (C) 1997 Elsevier Science B.V.

引用

页码：183 / 188

页数：6