Alice Y. Romans

TL;DR: The competition for the hydrophobic peptide of glycophorin, T(is), between sodium deoxycholate and a series of phospholipids is examined as a possible means of obtaining a quantitative measure of protein-lipid affinity and it is concluded that the T( is) peptide has a relative lipid affinity of phosphatidylinositol > phosphatIDylcholine > phosph atidylserine.

TL;DR: Computer analysis of the ESR spectra indicate that 4-5 moles of phospholipid are immobilized per mole of protein over a wide range of lipid-to-protein ratios, which appears mediated by both the polar headgroups and the hydrocarbon tails of the phospholIPid.

TL;DR: Increasing concentrations of tryptic insoluble peptide were added to sonicated small unilamellar egg phosphatidylcholine vesicles and the rate of efflux was examined, consistent with a mechanism to explain the fast Na + efflux component involving protein-lipid boundary perturbations.

TL;DR: Glycophorin was purified from human erythrocyte ghosts by the lithium diiodosalicylate -phenol procedure utilizing 125I-labeled lithium diioxycholate, and the preparation was found to contain 8.9 +/- 2.1 mol lithium diiosilicylate per mol glycophorins.