By Paul A. Hargrave, Klaus P. Hofmann, U. Benjamin Kaupp
This booklet bargains with the mechanism of sign transduction in vertebrate and invertebrate photoreceptors. It includes contributions at the constitution and serve as of rhodopsin or different G-coupled receptors, at the legislation of moment messengers by way of enzyme cascade, the position of Ca2+ in gentle variation, regulate of ionic channels in photoreceptor cells. a few key issues: Rhodopsin - constitution and serve as; transducin and phosphodiesterase; arrestin and kinase; cGMP-gated channel; position of Ca2+ in photoreceptors; transduction in invertebrates; eyes of halobacteria
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Extra info for Signal Transduction in Photoreceptor Cells: Proceedings of an International Workshop Held at the Research Centre Jülich, Jülich, Fed. Rep. of Germany, 8–11 August 1990
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1). Complete bleaching of the membranes causes the high temperature endotherm to almost completely disappear. 3 °C, when the average is taken for a large number of samples. When samples of membranes that have been bleached are subsequently incubated in the dark with 11-cis retinal, the high temperature endotherm reappears. On the basis of these experiments it is clear that the low temperature endotherm is due to opsin and the higher temperature endotherm is due to rhodopsin. If, following the thermal denaturation of opsin or rhodopsin, the samples are cooled and rescanned, the scans are completely flat (Fig.
Wavelength regulation consist of two elements: protonation of the Schiff-base link between LyS296 and ll-cis retinal, which in model compounds redshifts the peak absorbance from 360 to 440 nm, and spectral modulation which blue- or onward red-shifts the absorbance band anywhere in the spectral range 340-650 nm covered by vertebrate and invertebrate visual pigments. Fourthly, FTIR studies, investigating the confirmational changes triggered by light activation of rhodopsin, culminating in the formation of the active intermediate metarhodopsin II, have identified several peaks between 1720 and 1770 cm·1, which contribute to these changes, as representing protein-bound carboxy residues [38].
D. B. & Liou, G. I. (1982) Met. Enzymol. 81, 133-140. , van Osdol, W. , Mayorga, O. L. & Sanchez-Ruiz, J. M. (1990) in press Hargrave, P. A. (1982) Progress in Retinal Research (N. N. Osbourne and G. J. ) 1, 1-51. Hubbard, R. (1958) J. Gen. 42, 259-280. Khan, S. M. A. (1990) thesis, Southern Illinois University Khan, S. M. , Hargrave, P. , Santoro, M. M. & McDowell, J. H. (1991) Europ. J. Biochem. accepted for publication, Krebs, W. & Kuhn, H. (1977) Exp. Eye. Res. 25, 511-526. Kuhn, H. & Hargrave, P.
