Phospholipid content and activity of pure uridine diphosphate-glucuronyltransferase from rat liver.
Rat liver phospholipids were radioactively labeled in vivo before purification of UDP-glucuronyltransferase to homogeneity. The pure enzyme contained very little phospholipid (approx. 0.7 mol of phospholipid/mol of protein). The solubilization detergent Lubrol 12A9 appeared to act as a phospholipid substitute, capable of supporting UDP-glucuronyltransferase activity. Phospholipase C did not inhibit the pure enzyme activity and pure UDP-glucuronyltransferase was stimulated by 40--100% by the addition of phospholipid dispersions.
D000818:Animals; D003902:Detergents; D014453:Glucuronosyltransferase / Q000378:metabolism*; D008099:Liver / Q000201:enzymology*; D008297:Male; D010710:Phosphates / Q000032:analysis*; D051381:Rats
D003902:Detergents; D010710:Phosphates; D014453:Glucuronosyltransferase