Abstract
The effects of Triton X-100 on purple membrane have been examined for dark- and light-adapted membrane suspensions. Bacteriorhodopsin is more readily solubilized from dark-adapted than from light-adapted preparations, while light-dark adaptation does not influence phospholipid solubilization. Surfactant-induced changes in the absorption spectrum and retinal isomer distribution of bacteriorhodopsin are also illumination-dependent. These results are discussed in the light of structural data.
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