Phospholipid content and activity of pure uridine diphosphate-glucuronyltransferase from rat liver
- PMID: 96816
- PMCID: PMC1184033
- DOI: 10.1042/bj1710821
Phospholipid content and activity of pure uridine diphosphate-glucuronyltransferase from rat liver
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.
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