1. The properties of rhodopsin in solution have been examined in preparations from marine fishes, frogs, and mammals. 2. The bleaching of neutral rhodopsin in solution includes a photic and at least three thermal ("dark") processes. Thermal reactions account for approximately half the total fall in extinction at 500 mmicro. 3. Bleaching has been investigated at various pH's from 3.9 to about 11...

The transport of the photopigment rhodopsin from the inner segment to the photosensitive outer segment of vertebrate photoreceptor cells has been one of the main remaining mysteries in photoreceptor cell biology. Because of the lack of any direct evidence for the pathway through the photoreceptor cilium, alternative extracellular pathways have been proposed. Our primary aim in the present study...

An apparatus was constructed in order to record continuously and simultaneously changes in extinction and electrical conductance of rhodopsin solutions. With this apparatus, changes in electrical conductance on exposing rhodopsin to light were investigated. On illumination solutions of rhodopsin revealed a conductance change so long as they preserved their photosensitivity. The conductance chan...

The effects of light adaptation on the increment threshold, rhodopsin content, and dark adaptation have been studied in the rat eye over a wide range of intensities. The electroretinogram threshold was used as a measure of eye sensitivity. With adapting intensities greater than 1.5 log units above the absolute ERG threshold, the increment threshold rises linearly with increasing adapting intens...

The retina of the mosquito Aedes aegypti can be divided into four regions based on the non-overlapping expression of a UV sensitive Aaop8 rhodopsin and a long wavelength sensitive Aaop2 type rhodopsin in the R7 photoreceptors. We show here that another rhodopsin, Aaop9, is expressed in all R7 photoreceptors and a subset of R8 photoreceptors. In the dorsal region, Aaop9 is expressed in both the ...

Digitonin solutions of labelled rhodopsin, containing (3)H in the retinyl moiety, were prepared by two related methods. Labelled rhodopsin was also prepared for the first time in cetyltrimethylammonium bromide and purified by column chromatography. It was shown that only certain rhodopsin preparations on denaturation in the dark and the reduction with sodium borohydride gave up to 60% of the ra...

Rhodopsin is the primary molecule in the visual signaling cascade in vertebrate and invertebrate photoreceptor cells. Upon light absorption, the retinal chromophore in rhodopsin undergoes isomerization from the 11-cis to the all-trans configuration, which initiates the photoactivation process. In vertebrate retinas, the final photoproduct, meta-rhodopsin, activates a subtype of heterotrimeric G...

Rhodopsin is a G-protein-coupled receptor, in which retinal chromophore acts as inverse-agonist or agonist depending on its configuration and protonation state. Photostimulation of rhodopsin results in a pH-dependent equilibrium between the active state (Meta-II) and its inactive precursor (Meta-I). Here, we monitored conformational changes of rhodopsin using a fluorescent probe Alexa594 at the...

Two tests have been used to detect and to study conformational rearrangements of cattle rhodopsin, occurring in the process of rhodopsin photolysis and resulting in no change in the visual pigment absorption spectrum. The first test concerns the ability of retinal to react with hydroxylamine. This ability occurs after photoisomerization of retinal with a time constant of 0.3 s at 20 degrees C r...

Rhodopsin (rh1) is the visual pigment expressed in rod photoreceptors of vertebrates that is responsible for initiating the critical first step of dim-light vision. Rhodopsin is usually a single copy gene; however, we previously discovered a novel rhodopsin-like gene expressed in the zebrafish retina, rh1-2, which we identified as a functional photosensitive pigment that binds 11-cis retinal an...