Purification and properties of liver arginase from teleostean fish Clarias batrachus (L.).
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.
Singh
R A
RA
Department of Zoology, Banaras Hindu University, Varanasi, India.
Singh
S N
SN
D000818:Animals; D001119:Arginase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D002397:Catfishes / Q000378:metabolism*; D002845:Chromatography; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D008099:Liver / Q000201:enzymology*; D008970:Molecular Weight
D007527:Isoenzymes; D001119:Arginase