Extraction and liposome reconstitution of membrane proteins with their native lipids without the use of detergents

被引:35
作者
Smirnova, Irina A. [1 ]
Adelroth, Pia [1 ]
Brzezinski, Peter [1 ]
机构
[1] Stockholm Univ, Dept Biochem & Biophys, Arrhenius Labs Nat Sci, SE-10691 Stockholm, Sweden
基金
瑞典研究理事会;
关键词
CYTOCHROME-C-OXIDASE; MALEIC ACID COPOLYMER; FREE PURIFICATION; VESICLES; SOLUBILIZATION; DISTRIBUTIONS; SPECTRA; CHANNEL; BINDING; INTACT;
D O I
10.1038/s41598-018-33208-1
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Functional studies of membrane-bound channels, transporters or signal transducers require that the protein of interest resides in a membrane that separates two compartments. One approach that is commonly used to prepare these systems is to reconstitute the protein in liposomes. An intermediate step of this method is purification of the protein, which typically involves solubilization of the native membrane using detergent. The use of detergents often results in removal of lipids surrounding the protein, which may alter its structure and function. Here, we have employed a method for isolation of membrane proteins with a disc of their native lipids to develop an approach that allows transfer of the purified membrane protein to liposomes without the use of any detergents.
引用
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页数:6
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