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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 23 (1975), S. 20-24 
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of the American Chemical Society 93 (1971), S. 2308-2310 
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Analytical chemistry 36 (1964), S. 941-942 
    ISSN: 1520-6882
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular evolution 38 (1994), S. 250-262 
    ISSN: 1432-1432
    Keywords: Opsin ; Visual pigments ; Gene family ; Evolution ; Phylogeny ; Spectral sensitivity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Phylogenetic and physiological methods were used to study the evolution of the opsin gene family in Drosophila. A phylogeny based on DNA sequences from 13 opsin genes including representatives from the two major subgenera of Drosophila shows six major, well-supported clades: The “blue opsin” clade includes all of the Rhl and Rh2 genes and is separated into two distinct subclades of Rhl sequences and Rh2 sequences; the ultraviolet opsin clade includes all Rh3 and Rh4 genes and bifurcates into separate Rh3 and Rh4 clades. The duplications that generated this gene family most likely took place before the evolution of the subgenera Drosophila and Sophophora and their component species groups. Numerous changes have occurred in these genes since the duplications, including the loss and/or gain of introns in the different genes and even within the Rhl and Rh4 clades. Despite these changes, the spectral sensitivity of each of the opsins has remained remarkably fixed in a sample of four species representing two species groups in each of the two subgenera. All of the strains that were investigated had R1-6 (Rhl) spectral sensitivity curves that peaked at or near 480 nm, R7 (Rh3 and Rh4) peaks in the ultraviolet range, and ocellar (Rh2) peaks near 420 nm. Each of the four gene clades on the phylogeny exhibits very conservative patterns of amino acid replacement in domains of the protein thought to influence spectral sen sitivity, reflecting strong constraints on the spectrum of light visible to Drosophila.
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Journal of comparative physiology 91 (1974), S. 427-441 
    ISSN: 1432-1351
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Previous electroretinographic (ERG) studies of white-eyed and red-eyed (wild-type)Drosophila melanogaster (Stark and Wasserman, 1972a) yielded results that were in agreement with Goldsmith's (1965) hypothesis that eye-color pigment absorption decreases the recruitment of contributions from peripheral ommatidia into the ERG. These screening pigments therefore produce wavelength-specific differences between these two strains (as well as within the red-eyed strain) in three ERG parameters, namely the magnitudes of the on- and off-transients and the slopes of the receptor potential energy-response functions. In the present study these three ERG parameters were each measured for constant receptor potential magnitudes (to remove the contribution of spectral sensitivityper se) at 13 wavelengths from 350 nm to 650 nm in the following strains:cn (having only pterins),bw (having only ommatins), wild (having both pigment classes), and two white-eyed strains,cn bw andw. Multiple linear regression analyses were carried out in order to determine the relationships between the foregoing three ERG parameters and parameters related to spectral sensitivity. These data lead us to the following conclusions: 1. Unexpected wavelength-dependent parameter differences exist in white-eyed flies. The slopes of the energy-response functions and the magnitudes of the transients all systematically vary and all correlate highly with the spectral sensitivity and with each other. This result implicates another spectrally selective factor other than pigment-determined recruitment in the ERG ofDrosophila. Several hypotheses about the nature of this factor are discussed. 2. Parameter differences attributable strictly to eye-color pigments were found when wild,cn, andbw strains were compared with white-eyed strains. These parameter differences varied linearly with screening pigment density, and multiple linear regression analyses accurately predicted the differences in spectral sensitivity produced by the eye-color pigments from the parameter differences of transient sizes and energy-response function slopes.
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Journal of comparative physiology 96 (1975), S. 343-356 
    ISSN: 1432-1351
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Recent studies have indicated that intense short wavelength stimulation in flies converts rhodopsin to a longlived metarhodopsin while decreasing visual sensitivity and electroretinographic (ERG) responsivity. Long wavelength stimulation reverses both visual pigment and ERG alterations. In this study of ERG's in white-eyedDrosophila, spectral sensitivities were obtained following intense visible and ultraviolet short wavelength stimuli. Both stimuli decreased sensitivity to all wavelengths while ultraviolet light also selectively decreased ultraviolet sensitivity (Fig. 1). These results isolated three sensitivity components contributing to the ERG in flies: (1) the dark adapted sensitivity (Fig. 1); (2) the residual sensitivity remaining subsequent to intense ultraviolet stimulation (Fig. 1); and (3) the ultraviolet sensitivity specifically abolished by intense ultraviolet stimulation (Fig. 2). Further evidence shows that the three components are probably receptor-specific; the first two resemble recent fly receptor spectral sensitivity data (e.g. Eckert, 1971) while the third represents a separate ultraviolet receptor. Linear reciprocity of time and intensity to alter the ERG responsivity was found over considerable ranges for long wavelength (Fig. 3) and short wavelength (Fig. 4) induced responsivity alterations. ERG action spectra were obtained for altering responsivity (Fig. 5). The action spectrum for decreasing responsivity was roughly parallel with the dark adapted spectral sensitivity for wavelengths below 500 nm. The action spectrum for reestablishing responsivity had a peak near 570 nm and agreed with previous determinations of spectral characteristics of fly metarhodopsin. The action spectra determined were probably based on photopigment interconversions in the 1–6 receptor system. Long wavelength reconversion of metarhodopsin to rhodopsin may explain the high ultraviolet and low red sensitivities and the functional significance of red eye color pigments in flies.
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Journal of comparative physiology 121 (1977), S. 289-305 
    ISSN: 1432-1351
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Low vitamin A rearing decreases sensitivity and eliminates the ultraviolet but not the blue sensitivity maximum in R1-6 inDrosophila, Calliphora andMusca (Figs. 2–4). Spectral adaptation functions for control and vitamin A deprived flies yielded derived stable metarhodopsin absorption spectra from spectral sensitivity. Metarhodopsin has a long wavelength maximum and also has an ultraviolet maximum especially in the normal vitamin A condition (Figs. 2–4). M-potentials (fast early-receptor-like potentials) were obtained (Fig. 1) from all three genera in normal vitamin A rearing and were used for spectral adaptation studies (Figs. 2–3); the latter data are approximate inverses of sensitivity based spectral adaptation data. Thus, sensitivity must reflect proportion of rhodopsin, with metarhodopsin being inert in receptor potential generation. Vitamin A effects on spectral functions were further investigated inDrosophila. Ultraviolet (370 nm) and visible (470 nm) sensitivities varied approximately linearly with dietary vitamin A dose (Fig. 5); 370 nm sensitivity decreased more than 470 nm sensitivity at lower doses. Increasing adaptation intensities of 370 and 470 nm caused parallel decreases in spectral sensitivity assayed at 370 and 470 nm in normal vitamin A flies (Fig. 6); the adapting intensities were sufficient to convert photopigment. These and previous results suggest that the two R1-6 spectral peaks are ultimately mediated by one rhodopsin. R1-6 rhabdomeres were structurally similar in high and low vitamin A flies but emitted a long wavelength fluorescence to ultraviolet excitation in high vitamin A flies only (Fig. 7). These results suggest some form of energy transfer; i.e., a carotenoid may capture ultraviolet quanta and transfer energy to rhodopsin via inductive resonance. Spectral adaptation data are consistent with a calculated high rhabdomeric optical density of ECL=0.26 (i.e., 45% of incident light is absorbed) derived from presently available data onDrosophila. Calculations show electro-retinographic sensitivity to be extremely high, perhaps measurable at less than one absorbed quantum per rhabdomere.
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Journal of comparative physiology 126 (1978), S. 15-24 
    ISSN: 1432-1351
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Drosophila have 3 simple eyes, ocelli, located on the vertex of the head, in addition to 2 compound eyes. We determined ocellar function using the electroretinogram (ERG) and vision mutants. The ERG waveform in response to a 1 s stimulus was a slow negative (receptor depolarizing) potential followed by a return to baseline at light-off (Fig. 1). During long stimuli there was an exponential decay to baseline after the initial negative deflection. At light-off there was a positive overshoot and return to baseline (Fig. 2). During a long stimulus the ERG reflected stepwise changes in intensity, with a negative response to an increase in intensity and positive polarization to a decrease (Fig. 3). The ERG thus reflects extraction of intensity change information. The ocellar ERG waveforms (Fig. 4) and intensity-response functions (Fig. 5) were similar across wavelengths ranging from 370 to 520 nm. The ocellar spectral sensitivity peaks around 350–370 nm (ultraviolet) and 445 nm (blue) (Fig. 6). Chromatic adaptation with intense 370 or 445 nm did not selectively reduce 370 or 445 nm peak sensitivities (Fig. 7). These findings offer no support for more than one ocellar receptor type. In additional experiments, bright 570 nm adaptation was found to increase responsivity relative to bright short wavelength adaptation. These wavelength-specific effects were elicited even during anoxia suggesting wavelength-dependent photopigment interconversions (Fig. 8). Spectral adaptation data were obtained suggesting that ocelli have a stable (non-bleaching) metarhodopsin. Spectral adaptation and sensitivity data allowed an approximation of the metarhodopsin spectrum which has long wavelength and ultraviolet maxima (Fig. 7). Comparisons between the ERG waveforms and spectral sensitivities of normal and visual mutantDrosophila suggest that the absence of compound eye receptor types has no effect on the ocellar ERG. Also, strains with or without screening pigments do not show significant differences. However, 2 mutants with abnormal compound eye receptor potentials had ocellar abnormalities.
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Journal of comparative physiology 115 (1977), S. 47-59 
    ISSN: 1432-1351
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Receptor deficient mutants and chromatic adaptation were used to isolate the contribution of R7 to the electroretinogram (ERG) ofDrosophila. R7 was found to be a single-peaked ultraviolet (UV) receptor (Fig. 1). Photoconversion of the UV absorbing rhodopsin (R) to its stable 470–495 nm metarhodopsin (M) was shown to elicit a long-lived negative (depolarizing) afterpotential (Fig. 3) while inactivating R7. Photoreconversion ofM toR reactivates R7 (Fig. 2) and repolarizes the ERG (Fig. 3). The intensities of light needed to elicit afterpotentials by photointerconverting R7 photopigment were found to be about 2 log units greater than for R1-6 photopigment (Fig. 4). Vitamin A deprivation decreases R7 (as well as R8) sensitivity by about 2 log units (through decreased photopigment levels) without changing spectral sensitivity shape (Fig. 5). Vitamin A deprivation further eliminates the light-induced inactivation of R7 allowing experiments designed to characterize the in vivo spectral absorption of R7M. R7M was found to have UV and 495 nm maxima (Fig. 6). No polarization sensitivity was detected in the R7 ERG component. The adaptational properties of R7 are similar to the properties previously established for R1-6 but different from the properties of R8.
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Journal of comparative physiology 140 (1980), S. 275-286 
    ISSN: 1432-1351
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary We used microspectrophotometry, together with some associated electrophysiological measurements, to characterize the photopigments of R1–6 receptors in living, white-eyedDrosophila. Measurements were from the deep pseudopupil, an optical visualization of photopigment-containing rhabdomeres. Transmission changes associated with photointerconversion of rhodopsin (R480) and its stable metarhodopsin (M570) are easily seen (Fig. 1). Such transmission changes were measured to produce a difference specrum (Fig. 2); the isosbestic wavelength is about 502 nm. A photoequilibrium spectrum (Fig. 3), analyzed together with sensitivity data (Fig. 4a), was used to determine the fraction of M570 in photoequilibria established with various monochromatic wavelengths. From this, the quantum efficiency for M570 to R480 conversion relative to R480 to M570 efficiency was determined to be about 0.71. No dark regeneration of M570 to R480 occurred within a period of 60min (Fig. 4a, b). The extent of conversion related to incident energy was estimated as a function of wavelength (Figs. 5 and 6). These experiments yielded the photosensitivity spectrum of the visual pigment (Fig. 6). Assuming that the absorption spectrum of rhodopsin (R480) is the same as the sensitivity spectrum as determined by electrophysiology, this photosensitivity spectrum was used to derive the spectrum of metarhodopsin (M570) (Fig. 7). The maximal extinction of M570 is about 1.43 times the maximal extinction of R480. The spectra of both states of the photopigment fit the Ebrey-Honig nomogram in the long wavelength band. Both of the photosensitivity spectra, measured in the living eye, associated with R480 and M570 respectively have a major UV maximum.
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