Molecular and structural analysis of electrophoretic variants of soybean seed storage proteins |
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Authors: | Maruyama Nobuyuki Fukuda Takako Saka Shiori Inui Nauko Kotoh Junko Miyagawa Mayumi Hayashi Misa Sawada Machiko Moriyama Tatsuya Utsumi Shigeru |
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Affiliation: | Laboratory of Food Quality Design and Development, Graduate School of Agriculture, Kyoto University, Uji, Kyoto 611-0011, Japan. |
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Abstract: | Soybean (Glycine max L.) storage proteins are composed mainly of two major components, beta-conglycinin and glycinin. Electrophoretic variants of the beta subunit of beta-conglycinin and the A3 polypeptide of glycinin were detected on SDS-PAGE, and designated them as beta* and A3*, respectively. beta* and A3* exhibited higher and lower mobilities, respectively, than the common beta subunit and A3 polypeptide. The N-terminal nine and 10 amino acid sequences of beta* and A3* were completely identical to the previously reported sequences of the beta subunit and the A3 polypeptide, respectively. Analysis using concanavalin A-horseradish peroxidase and treatment with N-glycosidase indicated that glycans were not responsible for the difference in electrophoretic mobility of beta* or A3*. Furthermore, five clones of beta* or beta and three clones of A3*, respectively, were sequenced but we could not detect deletions and insertions except for a single or a few amino acid substitutions as compared with the common beta subunit and A3 polypeptide. These results indicate that a single or a few amino acid substitution affects the electrophoretic mobilities of beta* and A3*. |
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Keywords: | Leguminosae Soybean Seed storage protein Glycinin β-Conglycinin Electrophoretic variant Glycene max |
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