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- W41268129 abstract "Very few intrinsic membrane proteins have been purified to homogeneity. The main problem is not the lack of powerful separation methods but is instead the nonspecific aggregation that occurs as a consequence of the conditions used to solubilize and purify the proteins. To provide a rational basis for the choice of these conditions we examine here the effects of detergents, organic solvents (including ethylene glycol), acylation and ion pair formation, as well as the aggregation of (membrane) proteins caused by chromatographic and electrophoretic supporting media. Some properties of intrinsic membrane proteins are visualized by regarding the proteins as giant detergent molecules. The risk of denaturation by ionic detergents or organic solvents seems to be smaller the greater the hydrophobicity of the proteins (non-ionic detergents and deoxycholate are seldom denaturing)." @default.
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- W41268129 date "1982-01-01" @default.
- W41268129 modified "2023-10-15" @default.
- W41268129 title "Some General Aspects of the Difficulties to Purify Membrane Proteins" @default.
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- W41268129 doi "https://doi.org/10.1016/b978-0-08-027988-6.50007-0" @default.
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