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Thermal decomposition of rhodopsin, photoregenerated rhodopsin and P470
Vision Research, 1968Abstract The thermal stabilities of rhodopsin and photoregenerated rhodopsin in the temperature range 40–60°C are determined and found to be the same. The thermal decomposition of P470, produced by photolysis of metarhodopsin II, is measured in the temperature range 23–40°C.
B N, Baker, T P, Williams
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Vision Research, 1975
Iodoacetamide and its spin-labeled derivative in high concentration ranges (10−2−10−1M) react with unexposed SH-groups of rhodopsin in the dark. The spin-labels bound to these SH-groups are moderately immobilized. While rhodopsin is not spin-labeled with the iodoacetamide at a lower concentration (5 × 10−4 m) in the dark, photobleached rhodopsin is ...
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Iodoacetamide and its spin-labeled derivative in high concentration ranges (10−2−10−1M) react with unexposed SH-groups of rhodopsin in the dark. The spin-labels bound to these SH-groups are moderately immobilized. While rhodopsin is not spin-labeled with the iodoacetamide at a lower concentration (5 × 10−4 m) in the dark, photobleached rhodopsin is ...
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Biochemistry, 1983
The interactions between rhodopsin molecules in a micellar detergent solution (octyl glucoside) and in reconstituted phospholipid vesicles were studied in the dark and after bleaching. Resonance energy transfer measurements were used to monitor the proximity between rhodopsin monomers conjugated with a fluorescent donor or a fluorescent acceptor ...
H, Borochov-Neori +2 more
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The interactions between rhodopsin molecules in a micellar detergent solution (octyl glucoside) and in reconstituted phospholipid vesicles were studied in the dark and after bleaching. Resonance energy transfer measurements were used to monitor the proximity between rhodopsin monomers conjugated with a fluorescent donor or a fluorescent acceptor ...
H, Borochov-Neori +2 more
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Phosphorylation of rhodopsin: Most rhodopsin molecules are not phosphorylated
Biochemical and Biophysical Research Communications, 1974Abstract Phosphorylation of rod membrane proteins is a light-dependent reaction. Most rhodopsin molecules, however, are not phosphorylated. The protein that is highly phosphorylated (>3 moles phosphate per mole phosphorylated protein) appears to be a rhodopsin species that is different from the rest or is located in different parts of the rod ...
H, Shichi, R L, Somers, P J, O'Brien
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Deactivation of Photoactivated Rhodopsin by Rhodopsin-Kinase and Arrestin
Journal of Receptor Research, 1987Photoactivated rhodopsin (R) catalyses, by repetitively interacting with many copies of a guanosine nucleotide binding protein (transducin), the amplified binding of GTP to transducin molecules which then activate cyclic GMP phosphodiesterase. Electrophysiologists recently have shown that cyclic GMP keeps ion channels in the plasma membrane of the rod ...
H, Kühn, U, Wilden
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Rhodopsin and phototransduction
Journal of Photochemistry and Photobiology B: Biology, 1999Recent studies on rhodopsin structure and function are reviewed and the properties of vertebrate as well as invertebrate rhodopsin described. Open issues such as the 'red shift' of the absorbance spectra are emphasized in the light of the present model of the retinal-binding pocket. The processes that restore the rhodopsin content in photoreceptors are
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