Phospholipid content and activity of pure uridine diphosphate-glucuronyltransferase from rat liver.
作者信息
Burchell B, Hallinan T
出版信息
Biochem J. 1978 Jun 1;171(3):821-4. doi: 10.1042/bj1710821.
Abstract
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.
摘要
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