Zona pellucida-binding of boar sperm acrosin is associated with the N-terminal peptide of the acrosin B-chain (heavy chain)

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Caprine acrosin. Purification, characterization and proteolysis of the porcine zona pellucida.

Acrosin purified from an acidic extract of ejaculated goat spermatozoa migrated as a single 42,000-Mr band in SDS/polyacrylamide-gel electrophoresis. Reduction and alkylation of caprine acrosin produced two polypeptides, one of Mr 40,000 (heavy chain) and the other of Mr 3700 (light chain). The light chain purified by reversed-phase h.p.l.c. was a glycosylated octadecapeptide with an amino acid...

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Boar acrosin. I. Purification and preliminary characterization of a proteinase from boar sperm acrosomes.

Acrosin is a proteolytic enzyme used by sperm to digest a path through the zona pellucida of the ovum. In ejaculated sperm it is inactivated by a proteinase inhibitor from seminal plasma that also inhibits trypsin. This inhibitor is removed or inactivated during the residence in the female reproductive tract as a part of the capacitation process. The boar acrosin-inhibitor complex was partially...

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The interaction of boar sperm proacrosin with its natural substrate, the zona pellucida, and with polysulfated polysaccharides.

Boar sperm acrosin is an acrosomal protease with trypsin-like specificity, and it functions in fertilization by assisting sperm passage through the zona pellucida by limited hydrolysis of this extracellular matrix. In addition to a proteolytic active site domain, acrosin binds the zona pellucida at a separate binding domain that is lost during proacrosin autolysis. In this study, we quantitate ...

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The clinical significance of sperm-zona pellucida binding.

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Sperm N-acetylglucosaminidase is involved in primary binding to the zona pellucida.

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ژورنال

عنوان ژورنال: FEBS Letters

سال: 1990

ISSN: 0014-5793

DOI: 10.1016/0014-5793(90)80881-i