Purification and properties of pigeon kidney arginase (original) (raw)

2000

Abstract

198-200Arginase was isolated and purified from the kidneys of pigeon (Coulmba livia) using DEAE-Sepharose CL 6B chromatography, affinity chromatography on arginine-AH-Sepharose 4B and gel filtration on Sephadex G200 in presence of 2-mercaptoethanol. The enzyme migrated to the anode at pH 8.3 on polyacrylamide gel electrophoresis. The purified enzyme showed an average molecular mass of 179,000 daltons, optimal pH of 9.5 and temperature of 55°C and the energy of activation was found to be 10.14 kCal/mol. The Km for L-argininc was 5.0 mM. The purified enzyme was inhibited by excess product (4 mM ornithine). </span

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