Limited and specific proteolysis of the zona pellucida by acrosin.
The proteolytic action of boar sperm acrosin on its natural substrate, the zona pellucida, was investigated. Acrosin exhibited substrate specificity for the zona pellucida and differentially hydrolyzed the glycoprotein families composing the zona pellucida. In contrast to acrosin, trypsin was a less-specific protease in terms of zona pellucida hydrolysis.
D000176:Acrosin / Q000032:analysis / Q000378:metabolism / Q000494:pharmacology*; D000818:Animals; D010450:Endopeptidases / Q000494:pharmacology*; D005260:Female; D005306:Fertilization; D006023:Glycoproteins / Q000378:metabolism; D006868:Hydrolysis; D007700:Kinetics; D008297:Male; D010063:Ovum / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism*; D013094:Spermatozoa / Q000032:analysis; D013552:Swine; D014357:Trypsin / Q000494:pharmacology; D015044:Zona Pellucida / Q000378:metabolism*
D006023:Glycoproteins; D010450:Endopeptidases; D010447:Peptide Hydrolases; D000176:Acrosin; D014357:Trypsin