Hernández-Unzón H Y, Ortega-Delgado M L
Laboratorio de Bioquimica, Centro de Botánica, Colegio de Postgraduados, Chapingo, México.
Plant Foods Hum Nutr. 1988;38(3):211-23. doi: 10.1007/BF01092860.
The electrophoretic pattern of the untreated common bean globulin cv. Flor de Mayo had 7 protein fractions ranging from 620 to 120 kilodaltons (kd). The last molecular weight corresponds to the monomeric form. One of the objectives of the present work was to establish a comparison among denaturation by heat, sodium dodecyl sulphate (SDS) and dithiothreitol (DTT). At pH 6.0, two bands were resistant to heat treatment, after SDS treatment of the untreated globulin several bands disappeared and two new bands with 26 and 15 kd appeared. DTT did not change the electrophoretic pattern, due to the small quantity of free SH groups in the globulin. At pH 6.0, phaseolin is partly resistant to heat denaturation due to aggregation in an acidic environment. Isoelectrofocusing (IEF) and SDS polyacrylamide gel electrophoresis (SDS-PAGE) separated phaseolin into 10 protein fractions. The hypothesis is that phaseolin or globulin aggregation is due to the charge difference of fractions.
未经处理的菜豆球蛋白品种弗洛尔·德梅奥的电泳图谱有7个蛋白质组分，分子量范围为620至120千道尔顿（kd）。最后的分子量对应单体形式。本研究的目标之一是对热变性、十二烷基硫酸钠（SDS）变性和二硫苏糖醇（DTT）变性进行比较。在pH 6.0时，有两条带对热处理有抗性，未经处理的球蛋白经SDS处理后，几条带消失，出现了两条分子量为26 kd和15 kd的新带。由于球蛋白中游离巯基数量较少，DTT没有改变电泳图谱。在pH 6.0时，由于在酸性环境中聚集，菜豆蛋白对热变性有部分抗性。等电聚焦（IEF）和SDS聚丙烯酰胺凝胶电泳（SDS-PAGE）将菜豆蛋白分离成10个蛋白质组分。推测菜豆蛋白或球蛋白聚集是由于各组分电荷差异所致。
