Scotopic Spectral Sensitivity and the Absorbance of Visual Pigments in Isolated Visual Cells and in the Intact Retina

Author(s):  
James K. Bowmaker
Nature ◽  
1961 ◽  
Vol 190 (4776) ◽  
pp. 639-639 ◽  
Author(s):  
H. AUTRUM ◽  
D. BURKHARDT

1968 ◽  
Vol 51 (2) ◽  
pp. 125-156 ◽  
Author(s):  
George Wald

Extraction of two visual pigments from crayfish eyes prompted an electrophysiological examination of the role of visual pigments in the compound eyes of six arthropods. The intact animals were used; in crayfishes isolated eyestalks also. Thresholds were measured in terms of the absolute or relative numbers of photons per flash at various wavelengths needed to evoke a constant amplitude of electroretinogram, usually 50 µv. Two species of crayfish, as well as the green crab, possess blue- and red-sensitive receptors apparently arranged for color discrimination. In the northern crayfish, Orconectes virilis, the spectral sensitivity of the dark-adapted eye is maximal at about 550 mµ, and on adaptation to bright red or blue lights breaks into two functions with λmax respectively at about 435 and 565 mµ, apparently emanating from different receptors. The swamp crayfish, Procambarus clarkii, displays a maximum sensitivity when dark-adapted at about 570 mµ, that breaks on color adaptation into blue- and red-sensitive functions with λmax about 450 and 575 mµ, again involving different receptors. Similarly the green crab, Carcinides maenas, presents a dark-adapted sensitivity maximal at about 510 mµ that divides on color adaptation into sensitivity curves maximal near 425 and 565 mµ. Each of these organisms thus possesses an apparatus adequate for at least two-color vision, resembling that of human green-blinds (deuteranopes). The visual pigments of the red-sensitive systems have been extracted from the crayfish eyes. The horse-shoe crab, Limulus, and the lobster each possesses a single visual system, with λmax respectively at 520 and 525 mµ. Each of these is invariant with color adaptation. In each case the visual pigment had already been identified in extracts. The spider crab, Libinia emarginata, presents another variation. It possesses two visual systems apparently differentiated, not for color discrimination but for use in dim and bright light, like vertebrate rods and cones. The spectral sensitivity of the dark-adapted eye is maximal at about 490 mµ and on light adaptation, whether to blue, red, or white light, is displaced toward shorter wavelengths in what is essentially a reverse Purkinje shift. In all these animals dark adaptation appears to involve two phases: a rapid, hyperbolic fall of log threshold associated probably with visual pigment regeneration, followed by a slow, almost linear fall of log threshold that may be associated with pigment migration.


1972 ◽  
Vol 5 (3) ◽  
pp. 349-393 ◽  
Author(s):  
Stanley D. Carlson

Visual pigments are embedded in the disc membranes of the outer segments of vertebrate rods and cones and in the microvilli of invertebrate visual cells. The pigment molecule in both is a most fascinating aggregate of known (the ubiquitous II-cis isomer of vitamin A1 or A2-aldehyde = retinal1 or 2; Hubbard & Wald, 1952) covalently bonded to the unknown (a protein termed opsin) (Anderson, Hoffman & Hall, 1971). This conjugated molecule is called rhodopsin or dehydrorhodopsin (porphryopsin) when the prosthetic portion is retinall or 2 respectively. So sensitive is this sterically hindered, bent and twisted molecule to light that absorption of one photon can initiate its isomerization to the all trans form. This conformational change is but one (but the best known) of the factors leading to receptor membrane changes ushering in the visual impulse.


1975 ◽  
Vol 65 (2) ◽  
pp. 235-251 ◽  
Author(s):  
L Sperling ◽  
R Hubbard

Retinochrome is a photosensitive pigment located primarily in the inner portions of the visual cells of cephalopods. Its absorption spectrum resembles that of rhodopsin, but its chromophore is all-trans retinal, which light isomerizes to 11-cis, the reverse of the situation in rhodopsin. The 11-cis photoproduct of retinochrome slowly reverts to retinochrome in the dark. The chromophoric site of retinochrome is more reactive than that of most visual pigments: (a) Hydroxylamine converts retinochrome in the dark to all-trans retinal oxime + retinochrome opsin. (by Sodium borohydride reduces it to N-retinyl opsin. (c) Lambda max of retinochrome shifts from 500 to 515 nm as the pH is raised from 6 to 10, with a loss of absorption above pH 8; meanwhile above this PH a second band appears at shorter wavelengths with lambda max 375 nm. These changes are reversible. (d) If retinochrome is incubated with all-trans 3-dehydroretinal (retinal2) in the dark, some 3-dehydroretinochrome (retinochrome2, lambda max about 515 nm) is formed. Conversely, when retinochrome2, made by adding all-trans retinal2 to bleached retinochrome or retinochrome opsin, is incubated in the dark with all-trans retinal some of it is converted to retinochrome. Retinal and 3-dehydroretinal therefore can replace each other as chromophores in the dark.


2020 ◽  
Vol 206 (1) ◽  
pp. 71-84 ◽  
Author(s):  
Victor Govardovskii ◽  
Alexander Rotov ◽  
Luba Astakhova ◽  
Darya Nikolaeva ◽  
Michael Firsov

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