Lipid-protein interactions with the Na,K-ATPase

被引：34

作者：

Esmann, Mikael ^{[1
]}

Marsh, Derek

机构：

[1] Univ Aarhus, Inst Physiol & Biophys, Dept Biophys, Aarhus, Denmark

[2] Max Planck Inst Biophys Chem, Spekt Abt, D-37070 Gottingen, Germany

来源：

CHEMISTRY AND PHYSICS OF LIPIDS | 2006年 / 141卷 / 1-2期

关键词：

lipid-protein interactions; Na; K-ATPase; lipid selectivity; spin labels; ESR;

D O I：

10.1016/j.chemphyslip.2006.02.018

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

Studies of lipid interactions with membranous Na,K-ATPase by using electron spin resonance spectroscopy in conjunction with spin-labelled lipids are reviewed. The lipid stoichiometry, selectivity and exchange dynamics at the lipid-protein interface can be determined, in addition to information on the configuration and rotational dynamics of the protein-associated lipid chains. These parameters, particularly the stoichiometry and selectivity, are related directly to the intramembranous structure of the Na,K-ATPase, and can be used to check the integrity of extensively trypsinised preparations. (c) 2006 Elsevier Ireland Ltd. All rights reserved.

引用

页码：94 / 104

页数：11

共 45 条

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[2]

[Anonymous], 1982, LIPID PROTEIN INTERA

[3]

Microsecond motions of the lipids associated with trypsinized Na,K-ATPase membranes. Progressive saturation spin-label electron spin resonance studies [J].