Abstract
The incorporation of C 14 labelled methionine and glycine into rhodopsin of the bullfrog retina was studied following administration in vitro and in vivo. High radioactivity in rhodopsin solution was measured both in vitro and in vivo after administration of methionine, whereas no radioactivity was found after the application of glycine. Electrophoresis of a rhodopsin solution, which was obtained 6 days after the injection of radioactive methionine was carried out with an Oxoid acetate cellulose strip. The purplish band thus obtained was shown to be rhodopsin by means of its bleaching properties, protein staining and fluorescence. Coincidence of the distinct radioactive band with the rhodopsin band was demonstrated by contact radioautography, showing that the labelled methionine was actually incorporated into opsin molecule. The results are discussed with relation to the previous morphological studies of synthesis and migration of proteins in the visual cells.
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