Effect on uridine diphosphate glucuronyltransferase activity of depleting and restoring phospholipids to guinea-pig liver microsomal preparations.
Phospholipid depletion substantially inhibited the maximum demonstrable activities of the forward (glucuronidation) and reverse reactions of UDP-glucuronyltransferase towards p-nitrophenol in guinea-pig liver microsomal preparations. Dispersions of liver phospholipids restored activity, whereas non-phospholipid amphipaths failed to do so effectively. These results suggest that the system is probably phospholipid-dependent rather than conformationally constrained by phospholipids.
D000818:Animals; D014453:Glucuronosyltransferase / Q000378:metabolism*; D006168:Guinea Pigs; D006602:Hexosyltransferases / Q000378:metabolism*; D066298:In Vitro Techniques; D008862:Microsomes, Liver / Q000378:metabolism*; D009596:Nitrophenols; D010713:Phosphatidylcholines; D010740:Phospholipases / Q000494:pharmacology; D010743:Phospholipids / Q000378:metabolism*
D009596:Nitrophenols; D010713:Phosphatidylcholines; D010743:Phospholipids; D006602:Hexosyltransferases; D014453:Glucuronosyltransferase; D010740:Phospholipases