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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-).

molecular human reproduction

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]