Molecular and structural analysis of electrophoretic variants of soybean seed storage proteins
Molecular and structural analysis of electrophoretic variants of soybean seed storage proteins
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DOI：
10.1016/s0031-9422(03)00385-6
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发表时间：
2003-10-01
期刊：
影响因子：
3.8
通讯作者：
Utsumi, S
中科院分区：
文献类型：
--
作者：
Maruyama, N;Fukuda, T;Utsumi, S
大豆（Glycine max L.）贮藏蛋白主要由两种主要组分β-伴大豆球蛋白和大豆球蛋白组成。在SDS-PAGE上检测到β-伴大豆球蛋白的β亚基和大豆球蛋白的A3多肽的电泳变体，并将其分别命名为β * 和A3*。β * 和A3* 分别表现出比常见β亚基和A3多肽更高和更低的迁移率。β * 和A3* 的N-末端9和10个氨基酸序列分别与先前报道的β亚基和A3多肽的序列完全相同。使用伴刀豆球蛋白A-辣根过氧化物酶和N-糖苷酶治疗的分析表明，聚糖不负责β * 或A3* 的电泳迁移率的差异。此外，5个克隆的β * 或β和3个克隆的A3*，分别进行了测序，但我们不能检测到缺失和插入，除了一个或几个氨基酸取代相比，共同的β亚基和A3多肽。这些结果表明，单个或几个氨基酸取代影响β * 和A3* 的电泳迁移率。(C)2003 Elsevier Ltd.保留所有权利。
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*. (C) 2003 Elsevier Ltd. All rights reserved.