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Sedimentation of Bovine Rhodopsin—Digitonin Micelles

Nature New Biology volume 229, pages 250–252 (1971)Cite this article

Abstract

RHODOPSIN, the photo-sensitive pigment of vertebrate vision receptors, consists of the lipoprotein opsin bound to the 11-cis isomer of retinal. Light isomerizes the 11-cis configuration to the all-trans, which makes the pigment unstable, leading eventually to the dissociation of the retinal from the lipoprotein. The belief that these dark steps involve conformational changes in the lipoprotein moiety stems from spectroscopic measurements which show the disappearance of lipoprotein-chromophore interactions and from kinetic and thermodynamic considerations1–5, but more direct evidence has come from the changes in circular dichroism and optical rotatory dispersion which occur with bleaching6–9. There is also an increase of Stokes radius on bleaching11.

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Authors and Affiliations

  1. Chemistry Department and Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida, 32306

    N. L. INCARDONA & K. MILES

  2. Biological Sciences Department and Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida, 32306

    B. N. BAKER

Authors
  1. N. L. INCARDONA
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  2. K. MILES
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  3. B. N. BAKER
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INCARDONA, N., MILES, K. & BAKER, B. Sedimentation of Bovine Rhodopsin—Digitonin Micelles. Nature New Biology 229, 250–252 (1971). https://doi.org/10.1038/newbio229250a0

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