Photosensitivity spectrum of crayfish rhodopsin measured using fluorescence of metarhodopsin.
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منابع مشابه
Photosensitivity spectrum of crayfish rhodopsin measured using fluorescence of metarhodopsin
Discrepancies exist among spectral measurements of sensitivity of crayfish photoreceptors, their absorption in situ, and the number and absorption spectra of crayfish photopigments that are extracted by digitonin solutions. We have determined the photosensitivity spectrum of crayfish rhodopsin in isolated rhabdoms using long wavelength fluorescence emission from crayfish metarhodopsin as an int...
متن کاملPhotosensitivity Spectrum of Crayfish
Discrepancies exist among spectral measurements of sensitivity of crayfish photoreceptors, their absorption in situ, and the number and absorption spectra of crayfish photopigments that are extracted by digitonin solutions. We have determined the photosensitivity spectrum ofcrayfish rhodopsin in isolated rhabdoms using long wavelength fluorescence emission from crayfish metarhodopsin as an intr...
متن کاملThe contribution of a sensitizing pigment to the photosensitivity spectra of fly rhodopsin and metarhodopsin
Most of the photoreceptors of the fly compound eye have high sensitivity in the ultraviolet (UV) as well as in the visible spectral range. This UV sensitivity arises from a photostable pigment that acts as a sensitizer for rhodopsin. Because the sensitizing pigment cannot be bleached, the classical determination of the photosensitivity spectrum from measurements of the difference spectrum of th...
متن کاملSignaling states of rhodopsin. Formation of the storage form, metarhodopsin III, from active metarhodopsin II.
Vertebrate rhodopsin consists of the apoprotein opsin and the chromophore 11-cis-retinal covalently linked via a protonated Schiff base. Upon photoisomerization of the chromophore to all-trans-retinal, the retinylidene linkage hydrolyzes, and all-trans-retinal dissociates from opsin. The pigment is eventually restored by recombining with enzymatically produced 11-cis-retinal. All-trans-retinal ...
متن کاملHydrogen bonding changes of internal water molecules in rhodopsin during metarhodopsin I and metarhodopsin II formation.
Rhodopsin is a 7-helix, integral membrane protein found in the rod outer segments, which serves as the light receptor in vision. Light absorption by the retinylidene chromophore of rhodopsin triggers an 11-cis-->all-trans isomerization, followed by a series of protein conformational changes, which culminate in the binding and activation of the G-protein transducin by the metarhodopsin II (Meta ...
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ژورنال
عنوان ژورنال: Journal of General Physiology
سال: 1982
ISSN: 0022-1295,1540-7748
DOI: 10.1085/jgp.79.2.313