Organization of enzymes in human erythrocyte membranes
- 1 January 1966
- journal article
- research article
- Published by American Physiological Society in American Journal of Physiology-Legacy Content
- Vol. 210 (1) , 139-145
- https://doi.org/10.1152/ajplegacy.1966.210.1.139
Abstract
Studies were directed at determining whether there was a specific organization of enzymes in erythrocyte membranes. Membranes prepared in the absence of Mg++ which were disrupted by exposure to sonic vibrations on lipid-active agents underwent an increase in activity of phosphoglycerate kinase but not glyceraldehyde phosphate dehydrogenase. When membranes which were prepared in the presence of Mg++ were disrupted by sonic oscillations and lipid-active agents, there were relatively large increases in activity of both phosphoglycerate kinase and glyceraldehyde phosphate dehydrogenase. The data are interpreted as showing that membrane phosphoglycerate kinase was oriented toward the lipid core of the membrane, whereas membrane glyceraldehyde phosphate dehydrogenase was directed toward the interior of the srythrocyte. It is postulated that this organization of enzymes in erythrocyte membranes might function by providing ATP for pump ATPase.This publication has 10 references indexed in Scilit:
- STUDIES OF THE METABOLISM OF HUMAN ERYTHROCYTE MEMBRANES*Journal of Clinical Investigation, 1963
- IS HEMOGLOBIN AN ESSENTIAL STRUCTURAL COMPONENT OF HUMAN ERYTHROCYTE MEMBRANES?*Journal of Clinical Investigation, 1963
- The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytesArchives of Biochemistry and Biophysics, 1963
- Cation Transport and Structure of the Red-Cell Plasma MembraneCirculation, 1962
- Structure of the Plasma MembraneCirculation, 1962
- The Contribution of Sialic Acid to the Surface Charge of the ErythrocyteJournal of Biological Chemistry, 1962
- Human erythrocyte phosphoglycerides I. Quantification of plasmalogens, fatty acids and fatty aldehydesBiochimica et Biophysica Acta, 1962
- A Comparison of the Inhibition of Stromal Adenosinetriphosphatase and Inhibition of Sugar Permeability in ErythrocytesJournal of Cellular and Comparative Physiology, 1962
- Membrane Adenosine Triphosphatase as a Participant in the Active Transport of Sodium and Potassium in the Human ErythrocyteJournal of Biological Chemistry, 1960
- REGULATORY MECHANISMS IN CARBOHYDRATE METABOLISM .3. LIMITING FACTORS IN GLYCOLYSIS OF ASCITES TUMOR CELLS1959