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

Hoppe-Seyler's Zeitschrift fur physiologische Chemie ·Vol. 356 ·No. 12 ·1975-12-00 ·Pages 1931-6

Schiessler H, Schleuning WD, Fritz H

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.

MeSH Terms

Acrosin/pharmacology Animals Arginine Benzoylarginine Nitroanilide Binding Sites Cattle Endopeptidases Hydrolysis Insulin Kinetics Lysine Male Peptide Fragments Ribonucleases Swine Trypsin/pharmacology

Chemicals

Insulin Peptide Fragments Benzoylarginine Nitroanilide Arginine Ribonucleases Endopeptidases Acrosin Trypsin Lysine

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Schiessler H

Schleuning W D

Fritz H

Article Info

Journal

Hoppe-Seyler's Zeitschrift fur physiologische Chemie

Abbr.

Hoppe Seylers Z Physiol Chem

ISSN

0018-4888

DOI

10.1515/bchm2.1975.356.2.1931

Published

1975-12-00

Pages

1931-6

Language

English

Region

Germany

NLM ID

2985060R

Subset

External Links

PubMed source DOI: 10.1515/bchm2.1975.356.2.1931 View journal details

Analysis Services

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

Contact

WeChat Official Account