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The anionic conjugates of bilirubin and bile acids stimulate ATP hydrolysis by S ‐(dinitrophenyl)glutathione ATPase of human erythrocyte
Author(s) -
Singhal Sharad S.,
Sharma Rajendra,
Gupta Sanjiv,
Ahmad Hassan,
Zimniak Piotr,
Radominska Anna,
Lester Roger,
Awasthi Yogesh C.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80405-r
Subject(s) - lithocholic acid , chemistry , glutathione , bilirubin , biochemistry , atpase , bile acid , glucuronide , hydrolysis , atp hydrolysis , conjugate , metabolism , enzyme , biology , mathematics , endocrinology , mathematical analysis
These studies demonstrate that bilirubin‐ditaurate (an analog of bilirubin‐diglucuronide), lithocholic acid 3‐ O ‐sulfate, and lithocholic acid 3‐ O ‐glucuronide, which are believed to be transported from liver into bile through an active transport process stimulate ATP hydrolysis by purified dinitrophenylglutathione ATPase of human erythrocytes. The K m and V ma? values of the enzyme for these substrates are similar to those for dinitrophenylglutathione indicating the transport mechanisms for bilirubin conjugates, and anionic bile acid‐conjugates from hepatocytes to bile and transport of GSH‐conjugates from erythrocytes may be mediated by similar mechanisms.