The complete primary structure of three isoforms of a boar sperm-associated acrosin inhibitor.

Abstract:

:Acrosin inhibitors of seminal vesicle origin, after binding to their acceptor molecules on the anterior part of ejaculated sperm, are thought to be important capacitation factors, protecting zona binding sites during sperm uterine passage, and then dissociating to allow sperm binding to the zona pellucida of the oocyte. Each species so far tested possess an heterogeneous population of isoinhibitors which may display overlapping but not identical biological functions. Here we report the complete primary structure of three isoforms of a boar sperm-associated acrosin inhibitor, whose sequences are 90% identical to the seminal plasma counterpart. Despite this high analogy, the differences between the sperm-associated and the seminal plasma inhibitors may confer to them different physico-chemical properties which are postulated to be of functional importance.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Jonáková V,Calvete JJ,Mann K,Schäfer W,Schmid ER,Töpfer-Petersen E

doi

10.1016/0014-5793(92)80347-j

keywords:

subject

Has Abstract

pub_date

1992-02-03 00:00:00

pages

147-50

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(92)80347-J

journal_volume

297

pub_type

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