Burchell B, Hallinan T
Biochem J. 1978 Jun 1;171(3):821-4. doi: 10.1042/bj1710821.
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.
在将UDP-葡萄糖醛酸基转移酶纯化至同质之前,对大鼠肝脏磷脂进行体内放射性标记。纯酶所含磷脂极少(约0.7摩尔磷脂/摩尔蛋白质)。增溶去污剂Lubrol 12A9似乎起到磷脂替代物的作用,能够支持UDP-葡萄糖醛酸基转移酶的活性。磷脂酶C不抑制纯酶活性,添加磷脂分散体后,纯UDP-葡萄糖醛酸基转移酶的活性可被刺激40% - 100%。