The Glycophorin-phospholipid Interface in Recombined Systems. A 31P-nuclear Magnetic Resonance Study

Overview

Journal Biophys J

Publisher Cell Press

Specialty Biophysics

Date 1981 Feb 1

PMID 7225506

Citations 10

Authors

P L Yeagle

A Y Romans

Affiliations

Soon will be listed here.

Abstract

Glycophorin, the MN glycoprotein from the erythrocyte membrane, was recombined with egg phosphatidylcholine and with the total lipid extract from human erythrocyte membranes in a membranous form. 31P-nuclear magnetic resonance (NMR) spectra of the recombinants resembled spectra obtained from unsonicated phospholipid dispersions and biological membranes. The glycophorin/phospholipid ratio in these recombinants was varied from approximately 50:1 (lipid/protein) to 200:1, and 31P-NMR spectral intensities were obtained. Comparison of these intensities to that expected based on a pure phospholipid standard revealed that there were two phospholipid environments in the recombinants: one immobilized by the protein, and one slightly disordered and nonimmobilized. A relatively constant number of phospholipids were immobilized per glycophorin at all lipid/protein ratios studied.

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