Purification and characterization of dinitrophenylglutathione ATPase of human erythrocytes and its expression in other tissues.
S-(2,4-dinitrophenyl)glutathione (Dnp-SG) ATPase of human erythrocytes has been purified to apparent homogeneity by affinity chromatography. In reduced denaturing gels, the subunit Mr value of Dnp-SG ATPase was found to be 38,000. Dinitrophenyl glutathione (Dnp-SG) stimulated the hydrolysis of ATP by the purified enzyme whereas oxidized glutathione (GSSG) did not, indicating that Dnp-SG and GSSG are transported from the erythrocytes by different transporters. Results of Western blot analysis using the antibodies against Dnp-SG ATPase subunits indicated that the enzyme was expressed in human liver, lung, placenta and pancreas.
Sharma
R
R
Department of Human Biological Chemistry and Genetics, University of Texas Medical Branch, Galveston 77550.
Gupta
S
S
Singh
S V
SV
Medh
R D
RD
Ahmad
H
H
LaBelle
E F
EF
Awasthi
Y C
YC
D000251:Adenosine Triphosphatases / Q000302:isolation & purification* / Q000378:metabolism; D001693:Biological Transport, Active; D015153:Blotting, Western; D002846:Chromatography, Affinity; D004910:Erythrocyte Membrane / Q000201:enzymology*; D005978:Glutathione / Q000031:analogs & derivatives* / Q000378:metabolism; D006801:Humans; D008970:Molecular Weight; D011233:Precipitin Tests; D014018:Tissue Distribution
C030190:S-(2,4-dinitrophenyl)glutathione; D000251:Adenosine Triphosphatases; C068387:S-(dinitrophenyl)glutathione ATPase; D005978:Glutathione