Molecular and structural analysis of electrophoretic variants of soybean seed storage proteins
Nobuyuki Maruyama, Takako Fukuda, Shiori Saka, Nauko Inui, Junko Kotoh, Mayumi Miyagawa, Misa Hayashi, Machiko Sawada, Tatsuya Moriyama and Shigeru Ut
Phytochemistry , Volume 64, Issue 3 , October 2003, Pages 701-708
2003
บทคัดย่อ
Soybean (Glycine max L.) storage proteins are composed mainly of two major components, b-conglycinin and glycinin. Electrophoretic variants of the b subunit of b-conglycinin and the A3 polypeptide of glycinin were detected on SDS-PAGE, and designated them as b* and A3*, respectively. b* and A3* exhibited higher and lower mobilities, respectively, than the commonsubunit and A3 polypeptide. The N-terminal nine and 10 amino acid sequences ofb* and A3* were completely identical to the previously reported sequences of thesubunit 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 ofb* or A3*. Furthermore, five clones of b* or b 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 b subunit and A3 polypeptide. These results indicate that a single or a few amino acid substitution affects the electrophoretic mobilities ofb* and A3*.