The Structure and Orientation of a Membrane Protein
- 1 June 1973
- journal article
- research article
- Published by Taylor & Francis in Hospital Practice
- Vol. 8 (6) , 76-84
- https://doi.org/10.1080/21548331.1973.11707930
Abstract
A major integral protein, glycophorin, has been isolated intact from erythrocyte “ghosts” and shown to be a tripartite molecule that spans the entire membrane, having hydrophilic ends that protrude from both membrane surfaces and a hydrophobic embedded middle. Not only is this structure compatible with the need to mesh with a lipid bilayer but it appears ideally suited to function as a transmission belt across the membrane.Keywords
This publication has 5 references indexed in Scilit:
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- Major glycoprotein of the human erythrocyte membrane: Evidence for an amphipathic molecular structureArchives of Biochemistry and Biophysics, 1973
- THE STRUCTURE OF ERYTHROCYTE MEMBRANES STUDIED BY FREEZE-ETCHINGThe Journal of Experimental Medicine, 1972
- Chemical Characterization and Surface Orientation of the Major Glycoprotein of the Human Erythrocyte MembraneProceedings of the National Academy of Sciences, 1972
- Electrophoretic analysis of the major polypeptides of the human erythrocyte membraneBiochemistry, 1971