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Murakami Kiyofumi

Affiliate Master Yamaguchi University

Publish Date (<span class="translation_missing" title="translation missing: en.view.desc">Desc</span>)
Characterization of the blue protein in the shell pattern of Japanese littleneck clam (Ruditapes philippinarum ) was performed by purification using anion-exchange chromatography, amino acid analysis, molecular weight measurements, quantification of ferric ions, etc. Blue colored two components were found by anion exchange chromatography. The blue colored shell protein and the colorless mantle protein were found to be homologous to each other in amino acid composition; they are acidic proteins rich in aspartic acid and glutamic acid and that the isoelectric point of the blue protein was estimated as pI =3.96. The secondary structures of the blue protein were estimated as α-helix (28.6%), β-sheet (20.1%), and random coil (51.3%). From combination of molecular weight measurements and quantification of ferric ions, it was found that the blue protein is formed as trimer or tetramer from the monomer proteins of about 10 kDa by complexing with ferric ion. It was also found that there are two kinds of ferric ion existing states and that reducing agents decompose the blue colored trimer or tetramer into dimer or smaller units accompanying decolorization.
Creators : Murakami Kiyofumi Ohtawa Hiromi Tokuda Tomoe Kanebayashi Yasue Yasuda Yuko Waizumi Kenji Publishers : Faculty of Education, Yamaguchi University
日本理科教育学会全国大会要項 Volume 62 pp. 407 - 407
published_at 2012-08-11
Creators : Murakami Kiyofumi Fujimura Taihei Publishers : 日本理科教育学会
日本理科教育学会全国大会要項 Volume 61 pp. 173 - 173
published_at 2011-08-19
Creators : Murakami Kiyofumi Komatsu Yusuke Publishers : 日本理科教育学会