Erythrocyte membrane proteins: A modified gorter-grendel experiment
- 1 June 1979
- journal article
- research article
- Published by Springer Nature in The Journal of Membrane Biology
- Vol. 47 (2) , 185-193
- https://doi.org/10.1007/bf01876116
Abstract
The pressure-area isotherm and shear resistance of spectrin-actin monolayers indicate a close-packed structure at about 1.0 m2/mg protein. This surface area is equivalent to a thickness of about two monolayers at the erythrocyte membrane inner face. The maximum elasticity (lowest compressibility) occurs at 0.7 m2/mg protein, indicating the limit of reversible compression. The mechanical properties of the monolayers approximate those of the intact membrane, suggesting that the structures are similar and that these monolayers may account for many of thein vivo properties.This publication has 13 references indexed in Scilit:
- The Permeability of Adsorbed- and Spread-Membrane Protein (Spectrin-Actin) Films to IonsPublished by American Chemical Society (ACS) ,1980
- The viscoelastic properties of monolayers of red cell membrane proteinsJournal of Colloid and Interface Science, 1979
- The sub‐membrane reticulum of the human erythrocyte: A scanning electron microscope studyJournal of Supramolecular Structure, 1977
- The effect of cholesterol on the viscosity of protein-lipid monolayersChemistry and Physics of Lipids, 1976
- Spectrin: Current understanding of its physical, biochemical, and functional propertiesLife Sciences, 1976
- Membrane proteins and membrane rheology1Biorheology, 1975
- Water-soluble proteins of the human red cell membraneThe Journal of Membrane Biology, 1970
- Surface Area of Human Erythrocyte Lipids: Reinvestigation of Experiments on Plasma MembraneScience, 1966
- The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytesArchives of Biochemistry and Biophysics, 1963
- ON BIMOLECULAR LAYERS OF LIPOIDS ON THE CHROMOCYTES OF THE BLOODThe Journal of Experimental Medicine, 1925