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 Lettjournal_title
FEBS lettersauthors
Jonáková V,Calvete JJ,Mann K,Schäfer W,Schmid ER,Töpfer-Petersen Edoi
10.1016/0014-5793(92)80347-jkeywords:
subject
Has Abstractpub_date
1992-02-03 00:00:00pages
147-50issue
1-2eissn
0014-5793issn
1873-3468pii
0014-5793(92)80347-Jjournal_volume
297pub_type
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