Titlebook: Biochemistry and Physiology of Visual Pigments; Symposium Held at In Helmut Langer Conference proceedings 1973 Springer-Verlag Berlin Heide

Madison

書目名稱Biochemistry and Physiology of Visual Pigments影響因子(影響力)




書目名稱Biochemistry and Physiology of Visual Pigments影響因子(影響力)學(xué)科排名




書目名稱Biochemistry and Physiology of Visual Pigments網(wǎng)絡(luò)公開度




書目名稱Biochemistry and Physiology of Visual Pigments網(wǎng)絡(luò)公開度學(xué)科排名




書目名稱Biochemistry and Physiology of Visual Pigments被引頻次




書目名稱Biochemistry and Physiology of Visual Pigments被引頻次學(xué)科排名




書目名稱Biochemistry and Physiology of Visual Pigments年度引用




書目名稱Biochemistry and Physiology of Visual Pigments年度引用學(xué)科排名




書目名稱Biochemistry and Physiology of Visual Pigments讀者反饋




書目名稱Biochemistry and Physiology of Visual Pigments讀者反饋學(xué)科排名

悠然

Kortison-Sto?therapie bei multipler Sklerosen the absence of NADPH to release of all-trans retinaldehyde. The NADPH-dependent release of retinol is due to the action of a retinoldehydrogenase present in the rod sac membrane, which is capable of reduction of free retinaldehyde as well as of reductive hydrolysis of retinylidene aldimines (4, 5).

虛情假意

https://doi.org/10.1007/978-3-642-92189-6tly the denaturation of the protein has some effect upon the binding of the chromophoric group and it is of interest to see whether this weakening would affect the quantum yield of photobleaching of rhodopsin.

MAIM

https://doi.org/10.1007/978-3-662-36548-9e ref. 6), while a retina stripped away from its pigment epithelium then replaced and bleached regenerates as much as 55– 88% (cf. Kühne, 7). The amount regenerated appears somewhat lower when the retina is separated, bleached and then replaced, but it is still considerably more than in the isolated retina.

ASSET

,, (Fortsetzung und Schluss). — ,. — ,,result of visual pigment bleaching. Our recent studies (9, 10) indicate some of the metabolic requirements for rapid complete regeneration of photosensitive pigment in preparations of bleached bovine photoreceptors incubated with all-trans retinal.

DAMN

Chromophore Migration after Illumination of Rhodopsinn the absence of NADPH to release of all-trans retinaldehyde. The NADPH-dependent release of retinol is due to the action of a retinoldehydrogenase present in the rod sac membrane, which is capable of reduction of free retinaldehyde as well as of reductive hydrolysis of retinylidene aldimines (4, 5).

Abominate

The Effect of Urea upon the Photosensitivity of Bovine Rhodopsintly the denaturation of the protein has some effect upon the binding of the chromophoric group and it is of interest to see whether this weakening would affect the quantum yield of photobleaching of rhodopsin.

注視

Ebct207

dominant