Matern H, Matern S, Gerok W
J Biol Chem. 1982 Jul 10;257(13):7422-9.
Microsomal UDP-glucuronosyltransferase activity toward chenodeoxycholic acid and testosterone has been isolated from rat liver and appears to be homogeneous in sodium dodecyl sulfate gel electrophoresis and polyacrylamide gradient gel electrophoresis. The conjugating activities toward chenodeoxycholic acid and testosterone co-purified and showed identical mobilities in disc gel electrophoresis, indicating that chenodeoxycholic acid and testosterone are glucuronidated by a single form of enzyme. UDP-glucuronosyltransferase activities toward estrone, bilirubin, 4-nitrophenol, and morphine did not co-purify with the activity toward chenodeoxycholic acid and testosterone and were not detectable in the pure enzyme in the presence or absence of phospholipids. In addition to glucuronic acid conjugation, the enzyme is able to catalyze galacturonic acid conjugation of chenodeoxycholic acid and testosterone. The enzyme has a subunit Mr approximately 54,000 and in the presence of the stabilizing detergent chenodeoxycholic acid, it appears to exist as an aggregate with an apparent Mr = 318,000 as estimated by gel filtration and 316,000 by polyacrylamide gradient gel electrophoresis.
微粒体对鹅去氧胆酸和睾酮的UDP-葡萄糖醛酸基转移酶活性已从大鼠肝脏中分离出来，在十二烷基硫酸钠凝胶电泳和聚丙烯酰胺梯度凝胶电泳中似乎是均一的。对鹅去氧胆酸和睾酮的结合活性共纯化，并且在圆盘凝胶电泳中显示出相同的迁移率，表明鹅去氧胆酸和睾酮由单一形式的酶进行葡萄糖醛酸化。对雌酮、胆红素、4-硝基苯酚和吗啡的UDP-葡萄糖醛酸基转移酶活性与对鹅去氧胆酸和睾酮的活性没有共纯化，并且在有无磷脂存在的情况下，在纯酶中均未检测到。除了葡萄糖醛酸结合外，该酶还能够催化鹅去氧胆酸和睾酮的半乳糖醛酸结合。该酶的亚基Mr约为54,000，在稳定去污剂鹅去氧胆酸存在下，通过凝胶过滤估计其以Mr = 318,000的聚集体形式存在，通过聚丙烯酰胺梯度凝胶电泳估计为316,000。
