ACID-BASE PROPERTIES OF RHODOPSIN AND OPSIN
نویسندگان
چکیده
منابع مشابه
Acid-base Properties of Rhodopsin and Opsin
Purified preparations of cattle rhodopsin have been titrated to various pH, irradiated, and the pH changes followed thereafter until completed. In this way we have obtained the titration curves of rhodopsin, of the immediate product of irradiation, measured within 30 seconds; and of the final product of irradiation (opsin). The rhodopsin preparations display about 54 titratable groups per mole ...
متن کاملThe Thermal Stability of Rhodopsin and Opsin
Rhodopsin, the red photosensitive pigment of rod vision, is composed of a specific cis isomer of retinene, neo-b (11-cis), joined as chromophore to a colorless protein, opsin. We have investigated the thermal denaturation of cattle rhodopsin and opsin in aqueous digitonin solution, and in isolated rod outer limbs. Both rhodopsin and opsin are more stable in rods than in solution. In solution as...
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THE STABILITY OF CATTLE RHODOPSIN AND OF ITS PROTEIN MOIETY OPSIN TOWARD ACIDS AND ALKALIES AND ON AGING WAS DETERMINED BY TWO CRITERIA: maintenance of absorption spectrum, and capacity to regenerate after exposure to light. On storage at 3 degrees C. at pH near neutrality, the absorption spectrum in the visible region may remain unchanged for as long as 6 months; but the regenerability progres...
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in this thesis, at first we investigate the bounded inverse theorem on fuzzy normed linear spaces and study the set of all compact operators on these spaces. then we introduce the notions of fuzzy boundedness and investigate a new norm operators and the relationship between continuity and boundedness. and, we show that the space of all fuzzy bounded operators is complete. finally, we define...
15 صفحه اولTiie Thermal Stability of Rhodopsin and Opsin by Ruth Hubbard*
Rhodopsin, the red photosensitive pigment of rod vision, is composed of a specific cis isomer of retinene, neo-b (ll-c~s), joined as chromophore to a colorless protein, opsin. We have investigated the thermal denaturation of cattle rhodopsin and opsin in aqueous digitonin solution, and in isolated rod outer limbs. Both rhodopsin and opsin are more stable in rods than in solution. In solution as...
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ژورنال
عنوان ژورنال: Journal of General Physiology
سال: 1956
ISSN: 1540-7748,0022-1295
DOI: 10.1085/jgp.39.6.909