从正常和黄疸型冈恩大鼠中分离胆红素葡萄糖醛酸转移酶激活剂。

Isolation of an activator of bilirubin glucuronyltransferase from normal and jaundiced Gunn rats.

作者信息

Odell G B, Mogilevsky W S, Siegel F L

机构信息

Department of Pediatrics, University of Wisconsin School of Medicine, Madison 53792.

出版信息

Biochem Biophys Res Commun. 1988 Aug 15;154(3):1212-21. doi: 10.1016/0006-291x(88)90269-0.

DOI:10.1016/0006-291x(88)90269-0

PMID:3408494

Abstract

A microsomal activator of the UDP-glucuronyltransferase for bilirubin has been isolated from lubrol solubilized and salt fractionated liver microsomes. The activator has been partially purified by anion exchange and molecular sieving chromatography and found to have a molecular weight of about 60 kDa. The activator is present in liver from normal and bilirubin UDP-glucuronyltransferase deficient Gunn rats. When tested with purified UDP-glucuronyltransferase for bilirubin it accelerated the conjugation rate 10 fold but with the purified UDP-paranitrophenol transferase the rate of conjugation was increased only 1.5 times.

摘要

一种用于胆红素的UDP-葡萄糖醛酸基转移酶的微粒体激活剂已从用十二烷基月桂醇聚醚溶解并经盐分级分离的肝脏微粒体中分离出来。该激活剂已通过阴离子交换和分子筛色谱法进行了部分纯化，发现其分子量约为60 kDa。正常和胆红素UDP-葡萄糖醛酸基转移酶缺陷的冈恩大鼠的肝脏中均存在这种激活剂。当用纯化的胆红素UDP-葡萄糖醛酸基转移酶进行测试时，它使结合速率提高了10倍，但对于纯化的对硝基苯酚UDP-转移酶，结合速率仅提高了1.5倍。