Abstract
Glutathione- S-transferase from the cytosolic fraction of the bulb mite Rhizoglyphus robini has been purified to apparent homogeneity. The purification steps involved DEAE-Sepharose gel chromatography and glutathione-agarose affinity chromatography. The latter resulted in 94-fold purification and in 47% recovery of the enzyme activity present in the cytosol. The K m values for l-chloro-2,4-dinitrobenzene and reduced glutathione were calculated to be 0.13 and 0.26 mM, respectively. Sodium dodecyl sulphate-polyacrylamide electrophoresis revealed one polypeptide band of 25,000 daltons molecular weight.
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