Studies on the purification of rat liver uridine diphosphate glucuronyltransferase.
1. A stable, more highly purified, preparation of UDP-glucuronyltransferase was obtained than previously reported. 2. Enzyme activity towards o-aminophenyl and p-nitrophenyl was increased 43- and 46-fold respectively. 3. The final preparation contains only three staining polypeptide bands visible after sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. 4. The only known major accompanying protein appears to be epoxide hydratase. 5. The purified enzyme activity towards o-aminophenol can still be activated 3 fold by diethylnitrosamine. 6. On evidence from purification, o-aminophenol and p-nitrophenol appear to be glucuronidated by the same enzyme protein. The possible recognition of the UDP-glucuronyltransferase enzyme is discussed.
D000814:Aniline Compounds; D000818:Animals; D002852:Chromatography, Ion Exchange; D004052:Diethylnitrosamine; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D014453:Glucuronosyltransferase / Q000302:isolation & purification* / Q000378:metabolism; D008099:Liver / Q000201:enzymology*; D008297:Male; D008970:Molecular Weight; D009596:Nitrophenols; D051381:Rats
D000814:Aniline Compounds; D009596:Nitrophenols; D004052:Diethylnitrosamine; D014453:Glucuronosyltransferase