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result sql = Light damaging action of all-trans-retinal and its derivatives on rhodopsin molecules in the photoreceptor membrane.
Light damaging action of all-trans-retinal and its derivatives on rhodopsin molecules in the photoreceptor membrane.
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result sql = We have reproduced the model system containing A2-rhodopsin, NR-PE, A2-PE, and ATR-dimer-PE in order to study photosensitized damage of rhodopsin within photoreceptor membranes of rod outer segments. We have demonstrated that irradiation of such a system with visible light (400-700 nm) distorts the most important functional property of native visual pigment--its ability to regenerate after addition of 11-cis-retinal in the dark. We have also shown that all-trans-retinal bound to membrane phospholipids and rhodopsin has less photosensitizing activity that free all-trans-retinal.

Publication: Biochemistry Mosc. 2008 Feb ;73(2)::130-8.
Publication Date: 2008 Feb
Study Author(s): Loginova, M Yu;Rostovtseva, Ye V;Feldman, T B;Ostrovsky, M A;
Institution: Emanuel' Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, Russia. [email protected]
Shortcut link to this study:
We have reproduced the model system containing A2-rhodopsin, NR-PE, A2-PE, and ATR-dimer-PE in order to study photosensitized damage of rhodopsin within photoreceptor membranes of rod outer segments. We have demonstrated that irradiation of such a system with visible light (400-700 nm) distorts the most important functional property of native visual pigment--its ability to regenerate after addition of 11-cis-retinal in the dark. We have also shown that all-trans-retinal bound to membrane phospholipids and rhodopsin has less photosensitizing activity that free all-trans-retinal.
PMID: 18298368

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