The Interaction of Reduced Pyridine Nucleotides with the Red Cell Membrane
- 1 January 1969
- journal article
- Published by Taylor & Francis in Archives Internationales de Physiologie et de Biochimie
- Vol. 77 (2) , 251-259
- https://doi.org/10.3109/13813456909109705
Abstract
Introduction During the last decade, it has been gradually substantiated that the membrane was the site of energy metabolism in the mammalian erythrocyte. Indeed, all glycolytic enzymes have been found to be more or less firmly bound to the membrane in the human red cell (Green et al., 1965); on the other hand, ATP produced by glycolysis is utilized in the membrane as well, in order to allow active transport of cations (Hoffman, 1962 and Schatzmann, 1966) and probably some structural modifications of the erythrocyte (Nakao et al., 1960; Wins and Schoffeniels, 1966a).Keywords
This publication has 10 references indexed in Scilit:
- Possible involvement of electron transfer reactions in the (Mg+Ca)-dependent ATPase activity of red cell ghostsLife Sciences, 1968
- A ‘latent’ dinitrophenol-stimulated ATPase in red-cell ghostsBiochimica et Biophysica Acta (BBA) - Biomembranes, 1967
- Oscillatory states of mitochondriaArchives of Biochemistry and Biophysics, 1966
- Studies on red-cell ghost ATPase systems: Properties of a (Mg2+ + Ca2+-dependent ATPaseBiochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis, 1966
- ATP-dependent Ca++-Extrusion from human red cellsCellular and Molecular Life Sciences, 1966
- Nicotinamide-adenine dinucleotide dehydrogenase activity of human erythrocyte membranesBiochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis, 1966
- Association of integrated metabolic pathways with membranesArchives of Biochemistry and Biophysics, 1965
- The Active Transport of Sodium by Ghosts of Human Red Blood CellsThe Journal of general physiology, 1962
- Adenosine Triphosphate and Maintenance of Shape of the Human Red CellsNature, 1960
- PERMEABILITY PROPERTIES OF ERYTHROCYTE GHOSTSThe Journal of general physiology, 1952