Isolation of detergent-solubilized monomers of bacteriorhodopsin by size-exclusion high-performance liquid chromatography.

Academic Article


  • 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.
  • Published In

  • J Chromatogr  Journal
  • Keywords

  • Bacteriorhodopsins, Carotenoids, Chromatography, Gel, Chromatography, High Pressure Liquid, Detergents, Glucosides, Halobacterium, Micelles, Molecular Weight, Protein Denaturation, Spectrophotometry, Spectrophotometry, Ultraviolet, Temperature
  • Author List

  • Muccio DD; DeLucas LJ
  • Start Page

  • 243
  • End Page

  • 250
  • Volume

  • 326