Purification and Properties of Liver Arginase From Teleostean Fish Clarias Batrachus (L.)

Arch Int Physiol Biochim. 1990 Dec;98(6):411-9. doi: 10.3109/13813459009114003.

Abstract

Liver arginase of Clarias batrachus has been purified to 56.3-fold employing ammonium sulphate fraction, DEAE-cellulose and CM-cellulose chromatography. Bidirectional polyacrylamide gel electrophoresis shows the presence of two isoenzymes of arginase. The enzyme has a molecular weight of about 87,000 and Km 15.38 mM for L-arginine, optimum pH 9.5 and temperature 37 degrees C. Ornithine and leucine as competitive whereas valine and isoleucine act as non-competitive inhibitors with respect to L-arginine as substrate.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Arginase / chemistry
  • Arginase / isolation & purification*
  • Arginase / metabolism
  • Catfishes / metabolism*
  • Chromatography
  • Electrophoresis, Polyacrylamide Gel
  • Enzyme Stability
  • Hot Temperature
  • Hydrogen-Ion Concentration
  • Isoenzymes / chemistry
  • Isoenzymes / isolation & purification*
  • Isoenzymes / metabolism
  • Liver / enzymology*
  • Molecular Weight

Substances

  • Isoenzymes
  • Arginase