Purification and properties of liver arginase from teleostean fish Clarias batrachus (L.). |
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| Authors: | R A Singh S N Singh |
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| Institution: | Department of Zoology, Banaras Hindu University, Varanasi, India. |
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| 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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