[Modification of the retina photoreceptor membranes and temperature stability of rhodopsin].
The effect of modification of photoreceptor membranes of the bovine retina on the termodynamical parameters that characterize heat denaturation of rodopsin was studied. The highest increase of the rate constant and the corresponding maximal drop of the free energy change of heat denaturation of the pigment were obtained by using 7 M urea or 25% Triton X-100 in the presence of 5.10(-4) M EDTA. After chipping off one third of the protein from the rodopsin molecule by papain treatment a significant decrease of the slope of the Arrenius curve and a maximal decrease of entropy change compared to the parameters known for heat denaturation of the pigment in native photoreceptor membranes were found. Modification of the lipid components of the photoreceptor membranes (treatment with Triton X-100 and phospholipase C) reduced the thermostability of rodopsin. Maximal changes were obtained at Triton X-100 concentrations 0.1--1%, further concentration increas (1--25%) did not lead to significant changes. Phospholipase C treatment resulted in a decrease of free energy change and an increase of entropy change without affecting entalpy changes, accompaning the heat denaturation of rodopsin. Bivalent cations (Ca2+, Mg2+) increased the termostability of rodopsin both in photoreceptor membranes and in solutions to 25% Triton X-100.
D000818:Animals; D002413:Cations, Divalent; D002417:Cattle; D004355:Drug Stability; D010740:Phospholipases; D010786:Photoreceptor Cells / Q000648:ultrastructure*; D011092:Polyethylene Glycols; D011489:Protein Denaturation; D012160:Retina / Q000648:ultrastructure*; D012168:Retinal Pigments / Q000032:analysis; D012243:Rhodopsin / Q000032:analysis; D013696:Temperature; D013816:Thermodynamics
D002413:Cations, Divalent; D012168:Retinal Pigments; D011092:Polyethylene Glycols; D012243:Rhodopsin; D010740:Phospholipases
Modifikatsiia fotoretseptornykh membran setchatki i temperaturnaia stabil'nost' rodopsina.