Mapping the heparin-binding domain of boar spermadhesins.

Abstract:

:Boar spermadhesins are a group of seminal plasma, heparin-binding proteins which appear to be involved in sperm capacitation and gamete interaction. Using a proteolytic protection assay we have identified regions of AQN-1, AQN-3, PSP-I and AWN which remain attached to a heparin-Sepharose column following in-column digestion of bound spermadhesins with chymotrypsin and elastase. In addition, the complete amino acid sequence of spermadhesin AWN was synthesized as overlapping peptides, and their ability to bind to a heparin-Sepharose column and to inhibit the interaction of soluble heparin with purified ELISA plate-coated AWN was tested. Both approaches gave similar results and as a whole showed that different regions of AWN may converge in its tertiary structure to form a composite heparin-binding site. The conformational heparin-binding surface resides on the GFCC'C'' face of the proposed structural model for AWN and is in an opposite location to the carbohydrate-binding region of the spermadhesin.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Calvete JJ,Dostàlova Z,Sanz L,Adermann K,Thole HH,Töpfer-Petersen E

doi

10.1016/0014-5793(95)01513-2

subject

Has Abstract

pub_date

1996-02-05 00:00:00

pages

207-11

issue

3

eissn

0014-5793

issn

1873-3468

pii

0014-5793(95)01513-2

journal_volume

379

pub_type

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