Boar acrosin, I: modified isolation procedure, active-site titration and evidence for the presence of sialic acid.
Boar acrosin was isolated to electrophoretic homogeneity by modification of the method described by us previously.  Titration with p-nitrophenyl p-guanidinobenzoate revealed a molar activity of 8900 toward BzArgOEt and of 780 towards BzArgNHNp.  Treatment with neuraminidase led to an altered electrophoretic mobility, indicating that acrosin is sialogycoprotein
D000176:Acrosin / Q000032:analysis / Q000302:isolation & purification / Q000494:pharmacology; D000818:Animals; D001120:Arginine; D001586:Benzoylarginine Nitroanilide; D001665:Binding Sites; D010450:Endopeptidases; D004789:Enzyme Activation; D006023:Glycoproteins; D008297:Male; D008970:Molecular Weight; D012794:Sialic Acids / Q000032:analysis*; D013552:Swine
D006023:Glycoproteins; D012794:Sialic Acids; D001586:Benzoylarginine Nitroanilide; D001120:Arginine; D010450:Endopeptidases; D000176:Acrosin