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Light damaging action of all-trans-retinal and its derivatives on rhodopsin molecules in the photoreceptor membrane.
Loginova, M Yu; Rostovtseva, Ye V; Feldman, T B; Ostrovsky, M A.
Afiliação
  • Loginova MY; Emanuel' Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, Russia. marina.loguinova@mail.ru
Biochemistry (Mosc) ; 73(2): 130-8, 2008 Feb.
Article em En | MEDLINE | ID: mdl-18298368
ABSTRACT
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.
Assuntos
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Retinaldeído / Rodopsina / Segmento Externo da Célula Bastonete Idioma: En Revista: Biochemistry (Mosc) Ano de publicação: 2008 Tipo de documento: Article
Buscar no Google
Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Retinaldeído / Rodopsina / Segmento Externo da Célula Bastonete Idioma: En Revista: Biochemistry (Mosc) Ano de publicação: 2008 Tipo de documento: Article