Literature DB >> 1213688

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

H Schiessler, W D Schleuning, H 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.

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Year:  1975        PMID: 1213688     DOI: 10.1515/bchm2.1975.356.2.1931

Source DB:  PubMed          Journal:  Hoppe Seylers Z Physiol Chem        ISSN: 0018-4888


  2 in total

Review 1.  Proteases and proteolysis in the lysosome.

Authors:  P Bohley; P O Seglen
Journal:  Experientia       Date:  1992-02-15

2.  Transitional states of acrosomal exocytosis and proteolytic processing of the acrosomal matrix in guinea pig sperm.

Authors:  Kye-Seong Kim; James A Foster; Kevin W Kvasnicka; George L Gerton
Journal:  Mol Reprod Dev       Date:  2011-09-14       Impact factor: 2.609

  2 in total

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