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

Research output: Contribution to journalArticlepeer-review

50 Scopus citations


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
Issue number1
StatePublished - Feb 8 1988
Externally publishedYes


  • Dinitrophenylglutathione
  • Erythrocyte
  • Membrane
  • Transport

ASJC Scopus subject areas

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


Dive into the research topics of 'A novel dinitrophenylglutathione-stimulated ATPase is present in human erythrocyte membranes'. Together they form a unique fingerprint.

Cite this