文章基本信息

标题：Glycophorin in Lipid Bilayers
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作者：Chris W. M. Grant ; Harden M. McConnell
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1974
卷号：71
期号：12
页码：4653-4657
DOI：10.1073/pnas.71.12.4653
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Glycophorin, the major glycoprotein of human erythrocytes, has been isolated and reincorporated into lipid vesicles. Freeze-fracture electron microscopy shows the reincorporated glycophorin to occur as small particles in vesicle fracture faces while the etch faces are smooth. The glycoprotein has a tendency to cluster into groups of several particles. Evidence is presented that, although lipids in immediate contact with glycopherin are likely somewhat immobilized, the entire lipid-protein complex has a tendency to occupy fluid regions of the bilayer. Reincorporated glycophorin assumes its proposed conformation in the intact erythrocyte in so far as it penetrates the hydrophobic membrane interior while its N-terminal end with attached carbohydrate residues is exposed to the aqueous compartment and is available as a specific recognition site.
关键词：lipid-protein interactions ; freeze-fracture electron microscopy ; spin labels ; glycoproteins ; lateral phase separations