Phospholipid-dependence of oestrone UDP-glucuronyltransferase and p-nitrophenol UDP-glucuronyltransferase.
Hepatic UDP-glucuronyltransferase activity was resolved into two fractions, one exhibiting oestrone glucuronyltransferase activity and the other exhibiting p-nitrophenol glucuronyltransferase activity. Hydroxyapatite-column chromatography removed greater than 95% of the phospholipids from both preparations. The partially purified delipidated enzymes were essentially devoid of catalytic activity, but activities were restored by the addition of phospholipids or phosphatidylcholine mixtures containing various saturated and unsaturated fatty acids. Both oestrone and p-nitrophenol glucuronyl-transferase activities were reconstituted to similar degrees with the phosphatidylcholine mixtures. When purified phospholipids were tested, phosphatidylcholine and lysophosphatidylcholine were most effective in restoring activity, whereas phosphatidylethanolamine was the least effective. These results further suggest that oestrone and p-nitrophenol UDP-glucuronyltransferases are dependent on phospholipids for their activity.
D000818:Animals; D002848:Chromatography, DEAE-Cellulose; D002853:Chromatography, Liquid; D004970:Estrone / Q000378:metabolism*; D014453:Glucuronosyltransferase / Q000302:isolation & purification / Q000378:metabolism*; D066298:In Vitro Techniques; D008862:Microsomes, Liver / Q000201:enzymology; D009596:Nitrophenols / Q000378:metabolism*; D010743:Phospholipids / Q000378:metabolism*; D011092:Polyethylene Glycols; D011817:Rabbits
D009596:Nitrophenols; D010743:Phospholipids; D004970:Estrone; D011092:Polyethylene Glycols; D014453:Glucuronosyltransferase