The separation and purification of rat liver UDP-glucuronyltransferase activities towards testosterone and oestrone.
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.
D000818:Animals; D002848:Chromatography, DEAE-Cellulose; D004970:Estrone; D014453:Glucuronosyltransferase / Q000302:isolation & purification* / Q000378:metabolism; D008081:Liposomes; D008099:Liver / Q000201:enzymology*; D008722:Methods; D009596:Nitrophenols; D010713:Phosphatidylcholines; D051381:Rats; D013739:Testosterone
D008081:Liposomes; D009596:Nitrophenols; D010713:Phosphatidylcholines; D004970:Estrone; D013739:Testosterone; D014453:Glucuronosyltransferase