Purification of mouse liver UDPglucuronosyltransferase.

The present study describes a method for the purification of hepatic microsomal UDPglucuronosyltransferase from two different strains of mice, by a combination of detergent solubilization, ion-exchange chromatography and affinity chromatography. Using this procedure up to 0.5 mg of UDPglucuronosyltransferase could be obtained from 30 g of mouse liver and this enzyme could be purified from as little as 10 g of mouse liver. The molecular weight of the apparently homogeneous preparation was 57 000 +/- 2 000 when determined by sodium dodecyl sulphate polyacrylamide gel electrophoresis. The purified transferase catalysed the glucuronidation of approx. 0.6 mumol 4-nitrophenol min-1. mg-1 protein. Immunochemical analysis of this preparation further indicates that UDPglucuronosyltransferase has been purified to apparent homogeneity.