Chromatofocusing of glutathione S-transferases from human kidney

The glutathione S-transferase isoenzyme patterns of four human kidneys have been determined by chromatofocusing. The elution profiles were essentially similar in each tissue. Two major basic transferases and one acidic were partially characterized. All three were inhibited by bilirubin but considerable differences were found in the rate and extent of inactivation. The molecular weights, KM values and pH optima were similar to the values for transferases from other tissues. Chromatofocusing was found to be effective for the separation and purification of human glutathione transferases.