コウイカ(Sepia esculenta)の殼体を構成する有機物質

概要

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The soluble protein and the carbohydrate part separated chemically from the decalcified residue, and the undecalcified powder samples treated with hydrogenperoxide and base have been examined by amino acid, infrared and X-ray analyses for exploring the composition and the conformation of protein in the chitin-protein complex constituting the phragmocone of the cuttlebone of Sepia esculenta. The results suggest the following. 1. The composition of the insoluble protein differs from that of so called conchiolin-protein in the molluscan external shells. 2. The infrared spectrum of the soluble protein shows the conformation of protein may be almost the α-helix or random coils from the amido I absorption. 3. The infrared spectrum of the carbohydrate part shows that of chitin, but the small amount of amino acids are detected in this part. 4. The mineral component is only aragonite, and other mineral has not been recognized. Spacing values of the treated samples is not so different with one of the untreated cuttlebone. 5. The composition of the small amount of amino acids detected in the undecalcified samples treated with hydrogen-peroxide and base resembles that of so called conchiolin-protein, however does not show the characteristic pattern of the aragonitic shells.
地学団体研究会の論文
1975-05-20