Kinetic Attributes of Na+, K+ ATPase and Lipid / Phospholipid Profiles and Human Erythrocyte Membrane

Hetal G. Patel, Radha V. Aras, Surendra S. Katyare, Kunjan R. Dave

Research output: Contribution to journalArticlepeer-review

15 Scopus citations


Kinetic properties of Na+, K+ ATPase of membranes from rat and human erythrocytes were examined. The enzyme stability decreased with incubation time. The V(max) of the human enzyme was about 4 times lower than the values of the rat enzyme. However the energies of activation were higher. Phase transition temperature for the rat and the human enzyme was 24 °C and 17 °C, respectively. The human erythrocyte membranes were characterized by lower total phospholipid and cholesterol contents and were relatively more fluid. The human membranes contained lower proportions of acidic phospholipids which correlated well with the lower V(max) of the enzyme; the proportion of lysophosphoglyceride and sphingomyelin was higher in the human membrane.

Original languageEnglish (US)
Pages (from-to)770-777
Number of pages8
JournalZeitschrift fur Naturforschung - Section C Journal of Biosciences
Issue number9-10
StatePublished - Oct 2000


  • Erythrocyte Membrane
  • K ATPase
  • Na
  • Temperature and Substrate Kinetics

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry


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