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. 1983 Jul 15;132(2):324-7.
doi: 10.1016/0003-2697(83)90014-3.

Extraction of detergents from hydrophobic proteins with isopentanol: application to electrophoretic analysis of photosynthetic bacterial hydrophobic proteins

Extraction of detergents from hydrophobic proteins with isopentanol: application to electrophoretic analysis of photosynthetic bacterial hydrophobic proteins

J R Salcedo et al. Anal Biochem. .

Abstract

The method for extracting Triton X-100 used by I. H. Mather and C. B. Tampling [Anal. Biochem. 93, 139-142 (1979)], has been extended to other detergents of different charge and chemical nature. All the detergents tested can be extracted with isopentanol in conditions in which not more than 8% of hydrophobic or hydrophilic protein is lost from the water phase. The removal of detergent from reaction centers and light harvesting protein-pigment complexes of photosynthetic bacteria, eliminates the artifacts of oligomers when analyzed by sodium dodecyl sulfate-gel electrophoresis.

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