一种缺乏某些大豆球蛋白亚基的大豆品种的特性分析。

Characterization of a soybean cultivar lacking certain glycinin subunits.

作者信息

Staswick P E, Nielsen N C

出版信息

Arch Biochem Biophys. 1983 May;223(1):1-8. doi: 10.1016/0003-9861(83)90565-9.

Abstract

The 11S storage protein (glycinin) of soybean [Glycine max (L.) Merr., cv. Raiden] was studied by polyacrylamide gel electrophoresis and amino acid sequence analysis. It contained the following subunits composed of acidic (A) and basic (B) polypeptides: A1aB2, A1bB1b, A2B1a, and A3B4. However, it lacked polypeptides A4, A5, and B3 which are present in many other cultivars. A new acidic polypeptide called A6 was present in a low amount and was characterized by amino acid sequence analysis. It was homologous to A4, although of a smaller apparent molecular weight. Since Raiden has an average protein content of about 40% and its glycinin fraction can be purified as a 350,000 D complex which is typical of other cultivars, the results imply polymorphism with respect to glycinin subunit composition. Because there is a wide variation in the methionine content of the various subunits, these findings suggest the possibility of genetically manipulating the nutritional quality of soybean seed protein by altering glycinin subunit composition.

摘要

采用聚丙烯酰胺凝胶电泳和氨基酸序列分析方法，对大豆[Glycine max (L.) Merr., cv. Raiden]的11S贮藏蛋白（大豆球蛋白）进行了研究。它含有由酸性（A）和碱性（B）多肽组成的以下亚基：A1aB2、A1bB1b、A2B1a和A3B4。然而，它缺乏许多其他品种中存在的多肽A4、A5和B3。一种名为A6的新酸性多肽含量较低，并通过氨基酸序列分析对其进行了表征。它与A4同源，尽管表观分子量较小。由于Raiden的平均蛋白质含量约为40%，其大豆球蛋白组分可作为350,000 D的复合物纯化，这是其他品种的典型特征，结果表明大豆球蛋白亚基组成存在多态性。由于各种亚基的蛋氨酸含量存在很大差异，这些发现表明通过改变大豆球蛋白亚基组成来遗传操纵大豆种子蛋白营养品质的可能性。