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

Edward F. LaBelle, Shivendra V. Singh, Hassan Ahmad, Leszek Wronski, Satish K. Srivastava, Yogesh C. Awasthi

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Abstract

Vesicles prepared from human erythrocyte membranes were found to catalyze ATP hydrolysis that was stimulated by dinitrophenylglutathione (Dnp-SG). This activity was dependent on temperature and Me2+ and independent of ion pump ATPases present in erythrocyte membranes. The activity was a linear function of protein and time up to 60 min. The Km values of ATPase for Dnp-SG and ATP were found to be 49 μM and 1.67 mM, respectively. This suggests that in erythrocytes, the transport of Dnp-SG requires direct enzymatic hydrolysis of ATP and both Dnp-SG-stimulated ATPase activity and the ATP-dependent efflux of Dnp-SG from erythrocytes represent different activities of the same protein.

Original languageEnglish (US)
Pages (from-to)53-56
Number of pages4
JournalFEBS Letters
Volume228
Issue number1
DOIs
StatePublished - Feb 8 1988

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Keywords

  • Dinitrophenylglutathione
  • Erythrocyte
  • Membrane
  • Transport

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

LaBelle, E. F., Singh, S. V., Ahmad, H., Wronski, L., Srivastava, S. K., & Awasthi, Y. C. (1988). A novel dinitrophenylglutathione-stimulated ATPase is present in human erythrocyte membranes. FEBS Letters, 228(1), 53-56. https://doi.org/10.1016/0014-5793(88)80583-0