Isolation of detergent-solubilized monomers of bacteriorhodopsin by size-exclusion high-performance liquid chromatography.
Bacteriorhodopsin, an integral membrane protein of purple membranes, was solubilized with n-octylglucoside and isolated as intact monomeric micelles by high-performance size-exclusion chromatography. It was shown that separation was obtained between these micelles and either those containing bacterio-opsin or retinal as well as bacterio-opsin in the aggregated state. Estimates of the apparent molecular weights and Stokes radii were obtained by comparison with water-soluble proteins with known properties. Thermal denaturation of the native protein micelle induced the formation of a denatured species, which was similar to that found from denaturation at 4 degrees C.
D001436:Bacteriorhodopsins / Q000302:isolation & purification*; D002338:Carotenoids / Q000302:isolation & purification*; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D003902:Detergents; D005960:Glucosides; D006217:Halobacterium / Q000032:analysis; D008823:Micelles; D008970:Molecular Weight; D011489:Protein Denaturation; D013053:Spectrophotometry; D013056:Spectrophotometry, Ultraviolet; D013696:Temperature
D003902:Detergents; D005960:Glucosides; D008823:Micelles; C018619:octyl-beta-D-glucoside; D002338:Carotenoids; D001436:Bacteriorhodopsins; C017827:bacterio-opsin