| Literature DB >> 2144112 |
R Sharma1, S Gupta, S V Singh, R D Medh, H Ahmad, E F LaBelle, Y C Awasthi.
Abstract
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.Entities:
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Year: 1990 PMID: 2144112 DOI: 10.1016/0006-291x(90)91370-8
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575