Literature DB >> 7061043

Some properties of porcine carboxypeptidase N.

L Juillerat-Jeanneret, M Roth, J P Bargetzi.   

Abstract

Some properties of carboxypeptidase N purified from pig serum have been investigated. The amino acid composition resembles that of human carboxypeptidase N, but differs markedly from that of porcine carboxypeptidase B. The enzyme contains a mass fraction of 0.1 carbohydrates. Both ester and peptide substrates are hydrolyzed at the same site. Peptide substrates are hydrolyzed if lysine or arginine is the C-terminal amino acid, and provided that the penultimate amino acid is not proline. Argininic acid and epsilon-aminocaproic acid are good inhibitors of the enzyme.

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Year:  1982        PMID: 7061043     DOI: 10.1515/bchm2.1982.363.1.51

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


  1 in total

1.  Human and monkey lenses cultured with calcium ionophore form alphaB-crystallin lacking the C-terminal lysine, a prominent feature of some human cataracts.

Authors:  Emi Nakajima; Larry L David; Michael A Riviere; Mitsuyoshi Azuma; Thomas R Shearer
Journal:  Invest Ophthalmol Vis Sci       Date:  2009-07-15       Impact factor: 4.799

  1 in total

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