51. Molecular and structural analysis of electrophoretic variants of soybean seed storage proteins
- Author
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Mayumi Miyagawa, Junko Kotoh, Shigeru Utsumi, Tatsuya Moriyama, Takako Fukuda, Nobuyuki Maruyama, Shiori Saka, Misa Hayashi, Machiko Sawada, and Nauko Inui
- Subjects
Glycan ,Hot Temperature ,Glycoside Hydrolases ,Molecular Sequence Data ,Plant Science ,Horticulture ,Biochemistry ,Drug Stability ,Concanavalin A ,Protein Isoforms ,Storage protein ,Amino Acid Sequence ,Cloning, Molecular ,Molecular Biology ,Horseradish Peroxidase ,Glycoproteins ,chemistry.chemical_classification ,Calorimetry, Differential Scanning ,Sequence Homology, Amino Acid ,biology ,Seed Storage Proteins ,Globulins ,Amino acid substitution ,General Medicine ,Antigens, Plant ,Molecular biology ,Amino acid ,Protein Subunits ,Electrophoresis ,chemistry ,Seeds ,Glycine ,Soybean Proteins ,biology.protein ,Electrophoresis, Polyacrylamide Gel ,Soybeans ,Sequence Alignment ,Peroxidase - 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*.
- Published
- 2003