Purification and characterization of camel liver glutathione S-transferase

Abstract

Glutathione S-transferases have been purified (18-fold) in 65-70% yield from the liver of one humped camel using affinity chromatography on glutathione-linked agarose. Chromatofocusing technique resolves the glutathione S-transferases into seven distinct isoenzymes with apparent pI of 8.7, 8.4, 8.0, 7.8, 7.3 and 6.5. The major isoenzyme (pI 8.7) which accounted for over 95% of the total activity was composed of two identical subunits of molecular mass 24,000 and was immunologically similar to the other six isoenzymes. The substrate specificities and the effect of various inhibitors on the activity of the abundant camel liver isoenzyme were also examined.