Molecular weight of bacteriorhodopsin solubilized in Triton X-100.

Abstract
Bacteriorhodopsin from Halobacterium halobium was solubilized in the nonionic detergent Triton X-100. The circular dichroic spectrum and hydrodynamic properties indicate that the structure of this protein in the detergent is not significantly altered from that of the native membrane-bound form. Bacteriorhodopsin is monomeric under the conditions of solubilization with a MW of 24,250 .+-. 2000 and binds about 1 micelle of Triton X-100.