Department of Biochemistry, University of Ottawa, Ottawa, K1N 9B4 Canada.
Plant Physiol. 1985 Aug;78(4):812-6. doi: 10.1104/pp.78.4.812.
The globulins from wheat caryopses were found to consist primarily of protein sedimenting at approximately 3S and 7S. These proteins displayed a molecular weight distribution similar to that of the purified vicilin-like fractions from oat and pea, with variations occurring in the isoelectric points and relative quantities of their major subunits. concanavalin A Sepharose chromatography suggested that the major polypeptides of the wheat (3S + 7S) fraction are glycosylated. Western blot analysis using antioat (3S + 7S) globulin immunoglobulin G revealed the vicilins from pea and the globulin fractions of oat, wheat, barley, rye, corn, and rice to contain immunologically homologous polypeptides. Major groups of polypeptides were shared by all the cereals and pea, including subunits of approximately 75, 50, 40 kilodaltons and 20 to 25 kilodaltons. These results indicate that legume-like 3S and 7S globulins have been conserved and are being expressed in cereals.
从小麦胚乳中分离得到的球蛋白主要由沉降系数约为 3S 和 7S 的蛋白质组成。这些蛋白质的分子量分布与从燕麦和豌豆中分离得到的类似麦胚球蛋白的级分相似,只是其主要亚基的等电点和相对含量有所不同。刀豆球蛋白 A Sepharose 层析表明,小麦(3S+7S)级分中的主要多肽是糖基化的。用抗燕麦(3S+7S)球蛋白免疫球蛋白 G 进行的 Western blot 分析表明,豌豆中的麦胚球蛋白和燕麦、小麦、大麦、黑麦、玉米和水稻的球蛋白级分都含有免疫同源的多肽。所有谷物和豌豆都有共同的多肽,包括约 75、50、40 千道尔顿和 20 到 25 千道尔顿的亚基。这些结果表明,豆科植物样 3S 和 7S 球蛋白已被保存并在谷物中表达。