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1. Reconstitution of UDP-glucuronyltransferase preparations with phosphataidylcholine liposomes facilitated the purification of testosterone UDP-glucuronyltransferase. 2. Transferase activity towards testosterone co-purifies with that towards 4-nitrophenol. 3. UDP-glucuronyltransferase activity towards oestrone was separated from that towards testosterone. 4. These results suggest that testosterone and 4-nitrophenol may be glucuronidated by a different form of UDP-glucuronyltransferase from the one glucuronidating oestrone.

The separation and purification of rat liver UDP-glucuronyltransferase activities towards testosterone and oestrone