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ON RHODOPSIN IN SOLUTION

1. The properties of rhodopsin in solution have been examined in preparations from marine fishes, frogs, and mammals. 2. The bleaching of neutral rhodopsin in solution includes a photic and at least three thermal ("dark") processes. Thermal reactions account for approximately half the tota...

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Detalles Bibliográficos
Autor principal: Wald, George
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1938
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2141975/
https://www.ncbi.nlm.nih.gov/pubmed/19873085
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author Wald, George
author_facet Wald, George
author_sort Wald, George
collection PubMed
description 1. The properties of rhodopsin in solution have been examined in preparations from marine fishes, frogs, and mammals. 2. The bleaching of neutral rhodopsin in solution includes a photic and at least three thermal ("dark") processes. Thermal reactions account for approximately half the total fall in extinction at 500 mµ. 3. Bleaching has been investigated at various pH's from 3.9 to about 11. With increase in pH the velocity of the thermal components increases rapidly. Though the spectrum of rhodopsin itself is scarcely affected by change in pH, the spectra of all product-mixtures following irradiation are highly pH-labile. 4. The spectrum of pure rhodopsin—or of the rhodopsin chromophore—is fixed within narrow limits. The extinction at 400 mµ lies between 0.20 to 0.32 of that at the maximum. 5. Within the limitations of available data, the spectrum of pure rhodopsin corresponds in form and position with the spectral sensitivity of human rod vision, computed at the retinal surface. 6. The nature of bleaching of rhodopsin in solution, its kinetics, and its significance in the retinal cycle are discussed.
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spelling pubmed-21419752008-04-23 ON RHODOPSIN IN SOLUTION Wald, George J Gen Physiol Article 1. The properties of rhodopsin in solution have been examined in preparations from marine fishes, frogs, and mammals. 2. The bleaching of neutral rhodopsin in solution includes a photic and at least three thermal ("dark") processes. Thermal reactions account for approximately half the total fall in extinction at 500 mµ. 3. Bleaching has been investigated at various pH's from 3.9 to about 11. With increase in pH the velocity of the thermal components increases rapidly. Though the spectrum of rhodopsin itself is scarcely affected by change in pH, the spectra of all product-mixtures following irradiation are highly pH-labile. 4. The spectrum of pure rhodopsin—or of the rhodopsin chromophore—is fixed within narrow limits. The extinction at 400 mµ lies between 0.20 to 0.32 of that at the maximum. 5. Within the limitations of available data, the spectrum of pure rhodopsin corresponds in form and position with the spectral sensitivity of human rod vision, computed at the retinal surface. 6. The nature of bleaching of rhodopsin in solution, its kinetics, and its significance in the retinal cycle are discussed. The Rockefeller University Press 1938-07-20 /pmc/articles/PMC2141975/ /pubmed/19873085 Text en Copyright © Copyright, 1938, by The Rockefeller Institute for Medical Research This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Article
Wald, George
ON RHODOPSIN IN SOLUTION
title ON RHODOPSIN IN SOLUTION
title_full ON RHODOPSIN IN SOLUTION
title_fullStr ON RHODOPSIN IN SOLUTION
title_full_unstemmed ON RHODOPSIN IN SOLUTION
title_short ON RHODOPSIN IN SOLUTION
title_sort on rhodopsin in solution
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2141975/
https://www.ncbi.nlm.nih.gov/pubmed/19873085
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