从人肝脏中纯化并鉴定一种ATP酶，该酶在胆红素、胆汁酸和谷胱甘肽的结合物存在的情况下催化ATP水解。
Purification and characterization of an ATPase from human liver which catalyzes ATP hydrolysis in the presence of the conjugates of bilirubin bile acids and glutathione.
作者信息
Awasthi Y C, Singhal S S, Gupta S, Ahmad H, Zimniak P, Radominska A, Lester R, Sharma R
机构信息
Department of Human Biological Chemistry and Genetics, University of Texas Medical Branch, Galveston 77550.
出版信息
Biochem Biophys Res Commun. 1991 Mar 29;175(3):1090-6. doi: 10.1016/0006-291x(91)91677-5.
An ATPase has been purified from the membrane fraction of human liver which catalyzes ATP in the presence of bilirubin ditaurate, lithocholic acid 3-O-sulfate and lithocholic acid 3-O-glucuronide as well as dinitrophenylglutathione and other glutathione conjugates. Its subunit Mr value (38,000) and immunological properties are similar to dinitrophenylglutathione ATPase of human erythrocytes. Kinetic constants of the enzyme for the conjugates of glutathione, bile acids and bilirubin are comparable indicating that this ATPase may mediate active transport of all these anionic conjugates in liver.
已从人肝脏的膜组分中纯化出一种ATP酶，该酶在牛磺胆酸胆红素、石胆酸3 - O - 硫酸盐、石胆酸3 - O - 葡萄糖醛酸苷以及二硝基苯基谷胱甘肽和其他谷胱甘肽共轭物存在的情况下催化ATP。其亚基的分子量值（38,000）和免疫特性与人红细胞的二硝基苯基谷胱甘肽ATP酶相似。该酶对谷胱甘肽、胆汁酸和胆红素共轭物的动力学常数相当，表明这种ATP酶可能介导肝脏中所有这些阴离子共轭物的主动转运。
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