Affinity chromatography for the purification of glutathione S-transferase from Oxya chinensis
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Key Words：glutathione Stransferases (GSTs), Oxya chinensis, purification, affinity chromatography
Abstract： Glutathione Stransferase (GST) in the fifthinstar nymphs of Oxya chinensis（Thunberg）was purified by ammonium sulfate and GSHagrose affinity chromatography. Higher specific activity of GSTs could be detected at 60%-80% purity, and the highest specific activity was found at 90%. The specific activity was 0.3046 μmol/min/mg protein, and the purification factor was 1.82fold. Further GSHagrose affinity chromatography indicated that purification reached 50.88 with specific activity of 8.5185 μmol/min/mg protein. SDSPAGE analysis indicated that the purified GSTs preparation had a single band with a relative molecular mass of 25.4 ku. These results provide the basis for further study of the enzymatic properties, structural characteristics and functions of the GSTs of O. chinensis.