Cleavage specificity of boar acrosin on polypeptide substrates, ribonuclease and insulin B-chain.
The cleavage specificity of boar acrosin is, like that of trypsin, strictly limited to the arginyl and lysyl bonds, as demonstrated for the oxidized B-chain of insulin. In addition, in this polypeptide substrate as well as in reduced and carboxymethylated ribonuclease, these peptide bonds are hydrolyzed by acrosin and trypsin with nearly identical velocities.
D000176:Acrosin / Q000494:pharmacology; D000818:Animals; D001120:Arginine; D001586:Benzoylarginine Nitroanilide; D001665:Binding Sites; D002417:Cattle; D010450:Endopeptidases; D006868:Hydrolysis; D007328:Insulin; D007700:Kinetics; D008239:Lysine; D008297:Male; D010446:Peptide Fragments; D012260:Ribonucleases; D013552:Swine; D014357:Trypsin / Q000494:pharmacology
D007328:Insulin; D010446:Peptide Fragments; D001586:Benzoylarginine Nitroanilide; D001120:Arginine; D012260:Ribonucleases; D010450:Endopeptidases; D000176:Acrosin; D014357:Trypsin; D008239:Lysine