Abstract
The rhabdoms of Euphausia superba contain one digitonin-extractable rhodopsin, λmax 485 nm. The rhodopsin undergoes unusual pH-dependent spectral changes: above neutrality, the absorbance decreases progressively at 485 nm and rises near 370 nm. This change is reversible and appears to reflect an equilibrium between a protonated and an unprotonated form of the rhodopsin Schiff-base linkage. Near neutral pH and at 10°C, the rhodopsin is partially converted by 420-nm light to a stable 493-nm metarhodopsin. The metarhodopsin is partially photoconverted to rhodopsin by long-wavelength light in the absence of NH2OH; in the presence of NH2OH, it is slowly converted to retinal oxime and opsin. The rhodopsin of Meganyctiphanes norvegica measured in fresh rhabdoms by microspectrophotometry has properties very similar to those of the extracted rhodopsin of E. superba. Its λmax 488 nm and it is partially photoconverted by short wavelength irradiation to a stable photoconvertible metarhodopsin similar to that of E. superba. In the presence of light and NH2OH, the M. ncmegica metarhodopsin is converted to retinal oxime and opsin. Our results indicate that previous determinations of euphausiid rhodopsin absorbance spectra were incorrect because of accessory pigment contamination. © 1982, Rockefeller University Press., All rights reserved.
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CITATION STYLE
Denys, C. J., & Brown, P. K. (1982). Euphausiid visual pigments: The rhodopsins of euphausia superba and meganyctiphanes norvegica (Crustacea, Euphausiacea). Journal of General Physiology, 80(3), 451–472. https://doi.org/10.1085/jgp.80.3.451
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