蚕豆（Vicia faba L.）豆球蛋白的纯化及亚基结构
Purification and subunit structure of legumin of Vicia faba L. (broad bean).
作者信息
Wright D J, Boulter D
出版信息
Biochem J. 1974 Aug;141(2):413-8. doi: 10.1042/bj1410413.
Abstract
Zonal isoelectric precipitation was shown to be an effective method for the preparation of legumin which was homogeneous as judged by ultracentrifugation and polyacrylamide-gel electrophoresis. The subunit structure of legumin was investigated by preparative sodium dodecyl sulphate-polyacrylamide-gel electrophoresis and ion-exchange chromatography in urea. Five distinct subunits, of which two were acidic (alpha) and had a molecular weight of 37000, and three were basic (beta) with molecular weights of 20100, 20900 and 23800, were identified. The alpha and beta subunits were present in equimolar amounts in the legumin molecule and, in view of this and molecular-weight considerations, an alpha(6)beta(6) subunit model was proposed for legumin.
摘要
区域等电沉淀法被证明是制备豆球蛋白的有效方法，通过超速离心和聚丙烯酰胺凝胶电泳判断，该方法制备的豆球蛋白是均一的。通过制备性十二烷基硫酸钠-聚丙烯酰胺凝胶电泳和尿素中的离子交换色谱法研究了豆球蛋白的亚基结构。鉴定出五个不同的亚基，其中两个是酸性的（α），分子量为37000，三个是碱性的（β），分子量分别为20100、20900和23800。α和β亚基在豆球蛋白分子中以等摩尔量存在，鉴于此以及分子量方面的考虑，提出了豆球蛋白的α(6)β(6)亚基模型。
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