Abstract
(1) That retinaldehyde bound to a soluble protein can be extracted from the heads of honeybees is reasserted, and further evidence for this conclusion is presented. (2) A technique involving protein fractionation is described for partially purifying the retinaldehyde-protein complex. (3) As reported previously, the concentrated extract can be partially bleached by light, maximally at 440–450 nm. The difference spectra for dark bleaching with alkaline pH and with potassium borohydride show increases in absorption at 363 and 328 nm respectively, characteristic of retinaldehyde and retinol. (4) Evidence from spectral sensitivity measurements indicates that the 440 nm photopigment is probably not a native visual pigment. The chemical evidence, however, suggests that it may be a visual pigment (rhodopsin) with a modified tertiary structure. It is distinctly different from the light-sensitive ommochrome derivative present in the heads of bees and other insects.
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