Chromatographic resolution of the rod pigment from the four cone pigments of the chicken retina

Yen, Lei; Fager, Roger S.

doi:10.1016/s0042-6989(84)80005-x

Cited by 29 publications

(21 citation statements)

References 11 publications

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“…Both iodopsin and rhodopsin were purified from freshly dissected chicken retinas according to the method of Yen and Fager [6] with some modifications, the most important of which was the substitution of Chaps by digitonin, where 0.8-1.0 mg/ml PC was included to stabilize cone pigments. Detailed procedures will be described elsewhere.…”

Section: Methodsmentioning

confidence: 99%

“…Rhodopsin adsorbed to the column was selectively eluted with buffer A containing 100 mM (instead of 140 raM) NaCI, 0.6% Chaps, 0.8 mg/ml PC and 20% (w/v) glycerol. Only a small amount of other pigments was detected spectrophotometrically in either purified iodopsin (iodopsin/rhodopsin/short wavelength-sensitive pigments [6] = 90: 2 : 8) or purified rhodopsin (rhodopsin/ green-sensitive pigment = 96:4). lodopsin or rhodopsin thus obtained was incorporated into PC liposomes by dialysis against buffer B (10 mM Mops-NaOH, 2 mM MgC12, 140 mM NaC1, 1 mM DTT, 0.1 mM PhMeSO2F; pH 7.5) after adjusting the molar ratio of PC/pigment to 100.…”

Section: Methodsmentioning

confidence: 99%

“…However, no direct evidence has been presented so far that a cone pigment might expose a binding domain for T when irradiated. Although some cone pigments have been highly purified [6,7], the use of digitonin as a solubilizer has hampered biochemical investigations: since digitonin has a low critical micelle concentration and a high aggregation number, it is difficult to remove digitonin from purified proteins to prepare liposomes. We have recently succeeded in purifying one of the cone pigments, red-sensitive chicken iodopsin in Chaps (hmax: 571 nm) and in reconstituting it into phosphatidylcholine (PC) liposomes.…”

Section: Introductionmentioning

confidence: 99%

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Chicken red‐sensitive cone visual pigment retains a binding domain for transducin

Fukada¹,

Okano²,

Artamonov³

et al. 1989

FEBS Letters

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Iodopsin (a red-sensitive cone visual pigment) and rhodopsin (a rod pigment) were isolated from chicken retina. They were separately reconstituted into phosphatidylcholine liposomes and then mixed with rod transducin (Tot and TB~') purified from bovine retina, lodopsin enhanced, only when irradiated, the binding of GppNHp to T~t to a similar extent to irradiated rhodopsin. Furthermore, the binding of GppNHp to T~ in the presence of a photobleaching intermediate of iodopsin preferably required Tfly-2 rather than Tfly-l, which is very similar in profile to that in the presence of the intermediate of rhodopsin (J. Biol. Chem., in press). These results indicate that the binding domain for transducin in iodopsin should closely resemble that in rhodopsin.Cone visual pigment; Iodopsin; GTP-binding protein; Transducin; Rhodopsin; (Chicken retina)

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Chicken red‐sensitive cone visual pigment retains a binding domain for transducin

Fukada¹,

Okano²,

Artamonov³

et al. 1989

FEBS Letters

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“…Furthermore, it, like rhodopsin, has a high affinity for concanavalin A (8, 9), suggesting that its oligosaccharide chains are similar to those of rhodopsin. On the other hand, unlike rhodopsin, chicken green and the other chicken cone pigments are positively charged at neutral pH as shown by the lack of affinity for DEAE-Sepharose (8,9). In addition, chicken green and other cone pigments are unstable in the presence of hydroxylamine even in the dark (8,9).…”

mentioning

confidence: 99%

“…In fact, four kinds of cone visual pigments were extracted from chicken retinas (8,9). We determined absorption maxima of the pigments, which are located at 571 nm (chicken red), 508 nm (chicken green), 455 nm (chicken blue), and 415 nm (chicken violet) (9).…”

mentioning

confidence: 99%

Primary structures of chicken cone visual pigments: vertebrate rhodopsins have evolved out of cone visual pigments.

Okano

Kojima

Fukada

et al. 1992

Proc. Natl. Acad. Sci. U.S.A.

321

289

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Transcriptome profiling of developing photoreceptor subtypes reveals candidate genes involved in avian photoreceptor diversification

Enright

Lawrence

Hadžić

et al. 2014

J of Comparative Neurology

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Avian photoreceptors are a diverse class of neurons, comprised of four single cones, the two members of the double cone, and rods. The signaling events and transcriptional regulators driving the differentiation of these diverse photoreceptors are currently unknown. In addition, many distinctive features of photoreceptor subtypes, including spectral tuning, oil droplet size and pigmentation, synaptic targets and spatial patterning, have been well characterized, but the molecular mechanisms underlying these attributes have not been explored. To identify genes specifically expressed in distinct chicken (Gallus gallus) photoreceptor subtypes, we developed fluorescent reporters that label photoreceptor subpopulations, isolated these subpopulations using fluorescence-activated cell sorting and subjected them to next-generation sequencing. By comparing the expression profiles of photoreceptors labeled with rhodopsin, red opsin, green opsin, and violet opsin reporters, we have identified hundreds of differentially expressed genes that may underlie the distinctive features of these photoreceptor subtypes. These genes are involved in a variety of processes, including phototransduction, transcriptional regulation, cell adhesion, maintenance of intra- and extra-cellular structure, and metabolism. Of particular note are a variety of differentially expressed transcription factors, which may drive and maintain photoreceptor diversity, and cell adhesion molecules that may mediate spatial patterning of photoreceptors and act to establish retinal circuitry. These analyses provide a framework for future studies that will dissect the role of these various factors in the differentiation of avian photoreceptor subtypes.

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Chromatographic resolution of the rod pigment from the four cone pigments of the chicken retina

Cited by 29 publications

References 11 publications

Chicken red‐sensitive cone visual pigment retains a binding domain for transducin

Chicken red‐sensitive cone visual pigment retains a binding domain for transducin

Primary structures of chicken cone visual pigments: vertebrate rhodopsins have evolved out of cone visual pigments.

Transcriptome profiling of developing photoreceptor subtypes reveals candidate genes involved in avian photoreceptor diversification

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