Sulfhydryl binding reagents increase the conductivity of the light-sensitive channel and inhibit phototransduction in retinal rods
References (25)
- et al.
Transient sensitivity reduction and biphasic photoresponses observed when frog retinal rods are oxidized
Comp. Biochem. Physiol. A
(1987) - et al.
Effects of sulfhydryl binding reagents on the photoresponses of vertebrate retinal rods
Comp. Biochem. Physiol. A
(1989) Tissue sulfhydryl groups
Arch. Biochem. Biophys.
(1959)- et al.
Characterization of transducin from bovine rod outer segments
J. Biol. Chem.
(1984) - et al.
Real-time assay of rod disk membrane cGMP phosphodiesteraseand its controller enzymes
Methods Enzymol.
(1982) - et al.
Sulfhydryl group modification of photoreceptor G protein prevents it light-induced binding to rhodopsin
FEBS Lett.
(1984) - et al.
Characterization of a photoexposed sulfhydryl group of bovine rhodopsin available for chemical modification
Biochem. Biophys. Res. Commun.
(1974) - et al.
The isolation and purification of osmotically intact discs from retinal rod outer segments
Exp. Eye Res.
(1975) - et al.
The membrane current of single rod outer segments
J. Physiol. (Lond.)
(1979) - et al.
Light-sensitive swelling of isolated frog rod outer segments as an in vitro assay for visual transduction and dark adaptation
J. Gen. Physiol.
(1975)
The effect of phosphodiesterase inhibitors on the electrical activity of toad rods
J. Physiol. (Lond.)
The effects of phosphodiesterase inhibitors and lanthanum ions on the light-sensitive current of toad retinal rods
J. Physiol. (Lond.)
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Proteorhodopsin characterization based on metal-insulator-metal structure technique
2011, Thin Solid FilmsCitation Excerpt :The junctions show photoconductivity, as long as the retinal can isomerize, following light absorption. Biophysical characterization results support the assumption that the light-driven conductivity changes of the PR film might be associated with a photochemically induced M-like intermediate of PR [21,22]. We also tested PR (D97N) mutant [23,24] (data not shown) which does not produce an M-intermediate.
Cysteine-nitric oxide interaction and olfactory function
2002, Methods in EnzymologyCitation Excerpt :These results, taken together, suggest that the activation of the CNG channel by NO groups is by reduction of a free SH group without the subsequent formation of a disulfide bond. Moreover, the results described above, based on the use of sulfhydryl-modifying agents (IAA, NEM, and DTNB), suggest that the donor cysteine groups must be on the intracellular portion of the channel protein because, unlike NO, these reagents are only poorly membrane permeable,22 and so must have acted at the intracellular face of the membrane patch. In addition, application of a membrane-impermeant form of NEM, 1 mM dextran-NEM (kind gift of S. J. Kleene, University of Cincinnati; College of Medicine, Cincinnati, OH), can also activate the channel in inside-out patches.
Movement of gating machinery during the activation of rod cyclic nucleotide-gated channels
1998, Biophysical JournalCyclic nucleotide-gated channels
1997, Biomembranes: A Multi-Volume Treatise