Interaction of glycophorin with lipid bilayer studied by calorimetry, densitometry, static light scattering, and electron microscopy

Sen fang Sui, Erich Sackmann

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Abstract

In the first part of the present work the interaction of glycophorin with dimyristoylphosphatidylcholine (DMPC) is studied by freeze fracture electron microscopy, densitometry, calorimetry, and 90° static light scattering. An exothermic lipid/protein interaction energy of WP; =190kJ.mol-1 was found by application of the well known Van Laar relation for the displacement of the freezing point and the Gibbs-Duhem relationship. Secondly, the effects of Ca2+ on the lipid/protein interaction were studied. Following Ca2+ addition a remarkable decoupling of the interaction of the glycophorin head group with the bilayer surface was revealed by densitometry and gold-labeling electron microscopy. It is estimated that about 80% of lipid once disturbed by the adsorption of glycophorin head groups is decoupled after addition of Ca2+. Thirdly, the selective interaction of glycophorin with binary lipid mixtures was studied, including the mixtures of DMPC with dimyristoylphosphatidylserine (DMPS) and dilauroylphosphatidylcholine (DLPC), and the mixture of dipalmitoyl-phosphatidylcholine (DPPC) with DLPC.

Original languageEnglish
Pages (from-to)129-138
Number of pages10
JournalJournal of Biochemistry
Volume111
Issue number1
DOIs
StatePublished - Jan 1992

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