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-Reference-Cited by-同舟云学术

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

Published:1991-03 Issue:3 Volume:175 Page:1090-1096
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Awasthi Yogesh C.,Singhal Sharad S.,Gupta Sanjiy,Ahmad Hassan,Zimniak Piotr,Radominska Anna,Lester Roger,Sharma Rajendra

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference29 articles.

1. Transport of glutathioneS-conjugate from human erythrocytes

2. Detoxification of xenobiotics by glutathione S-transferases in erythrocytes: the transport of the conjugate of glutathione and 1-chloro-2,4-dinitrobenzene

3. Enzymatic conjugation of erythrocyte glutathione with 1-chloro-2,4- dinitrobenzene: the fate of glutathione conjugate in erythrocytes and the effect of glutathione depletion on hemoglobin

4. Dinitrophenyl glutathione efflux from human erythrocytes is primary active ATP-dependent transport

5. A novel dinitrophenylglutathione-stimulated ATPase is present in human erythrocyte membranes

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