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Comparative Study
. 1975 Dec;356(12):1931-6.
doi: 10.1515/bchm2.1975.356.2.1931.

Cleavage specificity of boar acrosin on polypeptide substrates, ribonuclease and insulin B-chain

H Schiessler, W D Schleuning, H Fritz
Comparative Study

Cleavage specificity of boar acrosin on polypeptide substrates, ribonuclease and insulin B-chain

H Schiessler et al. Hoppe Seylers Z Physiol Chem. 1975 Dec.

Abstract

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.

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