魚類インシュリンの過蟻酸酸化について

概要

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The oxidized bonito and tunny insulin have been studied by comparing paper electrophoresis in 20% formic acid and isoelectric fractionation in 0.1M aqueous ammonia with that of the oxidized beef insulin. Oxidation of these insulins were performed with performic acid under Sangers condition. After the electrophoresis the main three bands were present on paper in the oxidized fish insulin. One moved toward the anode and the other two toward the cathode, whereas the main two bands (A and B peptide chains) were present in the oxidized beef insulin (Fig. 1). This suggests that the fish insulin is probably composed of three peptide chains. When the oxidized fish insulin was fractionated in 0.1M aqueous ammonia at pH 5.5, the precipitate formed was small. The remaining fraction in the supernatant fluid showed the same three bands as the original oxidized insulin using the paper electrophoresis. Thus, the precipitation method for fractionation of the three peptide chains of the oxidized fish insulin was unsuccessful. Also, a comparison of the nitrogen content of the each bands separated after the electrophoresis of these oxidized insulins was conducted.
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