[Heat denaturation of opsin in warm-blooded animals as a possible mechanism of light-induced retinal damage].
The rate of thermal denaturation of bovine and rat opsin in the photoreceptor membranes was studied within a wide temperature range (between 37 and 70 degrees C). It was found that the rate of thermal denaturation of opsin at a physiological temperature (37 degrees C) might be commensurable or even exceed the known rate of rhodopsin renewal produced by photoreceptor disk formation and shedding. Lipid peroxidation caused an increase in the rate of opsin denaturation at a physiological temperature. It is assumed that accumulation of denatured opsin in the photoreceptor membranes during raised illumination together with lipid peroxidation induction may be one of the mechanisms leading to vision deterioration under raised illumination.
D000818:Animals; D002417:Cattle; D005136:Eye Proteins / Q000378:metabolism*; D006358:Hot Temperature; D007700:Kinetics; D008027:Light / Q000009:adverse effects*; D008054:Lipid Peroxides / Q000378:metabolism; D008297:Male; D010786:Photoreceptor Cells / Q000378:metabolism; D011489:Protein Denaturation; D051381:Rats; D011919:Rats, Inbred Strains; D012160:Retina / Q000528:radiation effects*; D012168:Retinal Pigments / Q000378:metabolism*; D012243:Rhodopsin / Q000378:metabolism; D017299:Rod Opsins; D013696:Temperature
D005136:Eye Proteins; D008054:Lipid Peroxides; D012168:Retinal Pigments; D017299:Rod Opsins; D012243:Rhodopsin
Teplovaia denaturatsiia opsina teplokrovnykh kak vozmozhnyĭ mekhanizm svetovogo porazheniia setchatki.