Abstract

The absorption spectra of intermediates formed from bullfrog rhodopsin during bleaching were determined in three kinds of preparations; digitonin extract, suspension of rod outer segments and retina. The spectra of rhodopsin and its intermediates in the extract differed in λ max, the relative extinction coefficient at the λ max and the half band width from those in the suspension. The spectra of the intermediates in the suspension were different only in their relative extinction coefficients from those in the retina. These relative extinction coefficients were used for computing the angles formed by the absorption vectors of the intermediates with respect to the disk membrane plane.

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