Small unilamellar vesicles containing glycophorin A. Chemical characterization and proton nuclear magnetic resonance studies.
Small unilamellar vesicles containing glycophorin A. Chemical characterization and proton nuclear magnetic resonance studies.
复制标题
含有血型糖蛋白 A 的小单层囊泡。化学表征和质子核磁共振研究。
DOI:
10.1021/bi00518a008
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发表时间:
1981
期刊:
影响因子:
2.9
通讯作者:
Prestegard,JH
中科院分区:
文献类型:
--
作者:
Ong,RL;Marchesi,VT;Prestegard,JH
Vesicles with as much as 1 molecule of protein per20 molecules of lipid can be prepared. Data on the vesicles obtained by using hydrolytic enzymes such as neuraminidase and trypsin, combined with amino acid analysis, suggest that glycophorin is incorporated in a transbilayer fashion with a high fractionof the molecules oriented with the carbohydrate-containing amino terminus to the vesicle exterior. In-teraction of the protein with the hydrophobic portion of the bilayer is apparent in proton nuclear magnetic resonance spectra, and lipid line-width increases have been used to characterize the strength and stoichiometry of interaction. Glycophorin is found to affect directly as many as 40 lipid molecules per molecule of protein; however, the magnitude of the effects is not large. e interaction of protein and lipid constituents of mem-branes is an important aspect of many membrane-centered phenomena. A variety of techniques have been employed, and a variety of lipid-protein systems studied, in an effort to elucidate the molecular details of those interactions [for a review, see Chapman et al.(1979)]. It is now apparent that a number of integralmembrane proteins may have hydrophobic segments of appropriate length tospan a lipid bilayer