PMID: 1213688Dec 1, 1975Paper

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

Hoppe-Seyler's Zeitschrift für physiologische Chemie
H SchiesslerH Fritz

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.

Citations

Feb 15, 1992·Experientia·P Bohley, P O Seglen
Sep 16, 2011·Molecular Reproduction and Development·Kye-Seong KimGeorge L Gerton
Mar 1, 1985·The Journal of Experimental Zoology·U A UrchJ L Hedrick
Dec 1, 1980·Hoppe-Seyler's Zeitschrift für physiologische Chemie·R Fock-NüzelH Fritz
Mar 30, 2021·Molecular Human Reproduction·Michael KuskeHagen Körschgen

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