Results 241 to 250 of about 85,236 (300)
Biotechnological production of natural pigments for textile dyeing. [PDF]
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Nature, 1967
Crayfish eye extracts contain two visual pigments resembling in spectrum vertebrate rhodopsin and iodopsin. In these crayfish, as in primates, the “iodopsin” appears to be the red sensitive pigment of colour vision.
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Crayfish eye extracts contain two visual pigments resembling in spectrum vertebrate rhodopsin and iodopsin. In these crayfish, as in primates, the “iodopsin” appears to be the red sensitive pigment of colour vision.
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Visual pigments and environmental light
Vision Research, 1984The visual pigments in the rods do not have a special absorption that gives them maximal sensitivity. The visual pigments of "deep sea" fish are an exception for these do match the environmental light to give maximum sensitivity. At the low light intensities at which the rods operate, it is the number of photons that go to make up each element of the ...
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Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1975
Abstract 1. 1. Harp ( Pagophilus groenlandicus ) and harbour ( Phoca vitulina ) seals had rod visual pigments with λ max of 496–497 nm. Grey seals ( Halichoerus grypus ) had a similar, if not identical visual pigment. 2. 2. The visual pigment from the northern fur seal ( Callorhinus ursinus ) appeared to have a λ max near 500 nm. 3.
D M, Lavigne, K, Ronald
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Abstract 1. 1. Harp ( Pagophilus groenlandicus ) and harbour ( Phoca vitulina ) seals had rod visual pigments with λ max of 496–497 nm. Grey seals ( Halichoerus grypus ) had a similar, if not identical visual pigment. 2. 2. The visual pigment from the northern fur seal ( Callorhinus ursinus ) appeared to have a λ max near 500 nm. 3.
D M, Lavigne, K, Ronald
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Science, 1968
The fluorescence of cattle rod outer segments (dried) and of rhodopsin in solution lies in the range of 575 to 600 millimicrons with a quantum efficiency of 0.005 if excitation is in the visible band near 500 millimicrons. The emission is abolished by bleaching at -196°C but can be reversibly regenerated by irradiation with light of longer wavelength ...
A V, Guzzo, G L, Pool
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The fluorescence of cattle rod outer segments (dried) and of rhodopsin in solution lies in the range of 575 to 600 millimicrons with a quantum efficiency of 0.005 if excitation is in the visible band near 500 millimicrons. The emission is abolished by bleaching at -196°C but can be reversibly regenerated by irradiation with light of longer wavelength ...
A V, Guzzo, G L, Pool
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Vision Research, 1971
Abstract Cone pigments in protanopes and deuteranopes were measured by retinal densitometry, and the energy of various monchromatic lights found that bleached at a fixed rate of 25 per cent total pigment per minute. The same bleaching lights were matched with a fixed yellow in a bipartite field. Lights matched for bleaching were found to look equally
D E, Mitchell, W A, Rushton
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Abstract Cone pigments in protanopes and deuteranopes were measured by retinal densitometry, and the energy of various monchromatic lights found that bleached at a fixed rate of 25 per cent total pigment per minute. The same bleaching lights were matched with a fixed yellow in a bipartite field. Lights matched for bleaching were found to look equally
D E, Mitchell, W A, Rushton
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Vision Research, 1971
Abstract Visual pigments from marine cetaceans, as in other mammals, are homogeneous and based on the retinal-l chromophore, but show a wider range in absorption maxima. Maxima range from 497 to 486 nm and for one species to 481 nm, but with less certainty. This distribution correlates best with the dominant hue present in the habitat of each species.
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Abstract Visual pigments from marine cetaceans, as in other mammals, are homogeneous and based on the retinal-l chromophore, but show a wider range in absorption maxima. Maxima range from 497 to 486 nm and for one species to 481 nm, but with less certainty. This distribution correlates best with the dominant hue present in the habitat of each species.
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Photointermediates of visual pigments
Journal of Bioenergetics and Biomembranes, 1992Much progress has been made in recent years toward understanding the interactions between various proteins responsible for visual transduction which are initiated by an activated state of visual pigments. However, the changes which take place in the visual pigments themselves to convert them to the activated state are more poorly understood.
J W, Lewis, D S, Kliger
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