Extraction of detergents from hydrophobic proteins with isopentanol: application to electrophoretic analysis of photosynthetic bacterial hydrophobic proteins.
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.
D001426:Bacterial Proteins / Q000302:isolation & purification*; D003902:Detergents / Q000302:isolation & purification*; D004586:Electrophoresis / Q000379:methods; D008565:Membrane Proteins / Q000302:isolation & purification; D000439:Pentanols; D013501:Surface-Active Agents / Q000302:isolation & purification*
D001426:Bacterial Proteins; D003902:Detergents; D008565:Membrane Proteins; D000439:Pentanols; D013501:Surface-Active Agents; C029683:isopentyl alcohol