Molecular weight of bacteriorhodopsin solubilized in Triton X-100.

AUTOR(ES)

Reyenolds, J A

RESUMO

Bacteriorhodopsin from Halobacterium halobium has been 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 molecular weight of 24,250+/-2,000 and binds approximately one micelle of Triton X-100.

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