Localization of a 25 kDa human sperm surface protein: its role in in- vitro human sperm capacitation [published erratum appears in Mol Hum Reprod 1997 Jul;3(8):638]
Author(s) -
Mayukh Banerjee
Publication year - 1997
Publication title -
molecular human reproduction
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.143
H-Index - 122
eISSN - 1460-2407
pISSN - 1360-9947
DOI - 10.1093/molehr/3.2.109
Subject(s) - biology , sperm , capacitation , in vitro , sialic acid , glycoprotein , hum , andrology , microbiology and biotechnology , biochemistry , genetics , medicine , art , performance art , art history
A human endometrial sialic acid-binding glycoprotein (SABP) binds specifically to a 25 kDa protein on the plasma membranes of human non-capacitated sperm heads. In-vitro labelling of the sperm surface sialoglycoconjugates and subsequent incubation with SABP, suggests removal of some sialoglycoconjugate moieties from the sperm surface upon interaction with SABP. SABP also induces the exposure of mannose ligand receptors on the sperm surface and increases the production of superoxide anion (O2-).
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