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  • Title: Purification and properties of liver arginase from teleostean fish Clarias batrachus (L.).
    Author: Singh RA, Singh SN.
    Journal: Arch Int Physiol Biochim; 1990 Dec; 98(6):411-9. PubMed ID: 1705780.
    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.
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