Dalgalarrondo M, Raymond J, Azanza J L
Biochimie. 1985 Jun;67(6):629-32. doi: 10.1016/s0300-9084(85)80203-0.
The subunit heterogeneity of the globulin fraction of sunflower seeds was investigated by two dimensional electrophoresis, using isoelectric focusing in the first dimension and sodium dodecyl sulphate polyacrylamide gel electrophoresis in the second dimension. Under non reducing conditions, intermediary subunits B, C and D (molecular weight 54 000, 48 000 and 40 000, respectively) were focused within a pI range 5.4-6.0 but intermediary subunits A (molecular weight 60 000) focused within a pI range 6.3-6.8. Under reducing conditions the electrophoretic patterns show that intermediary subunits consist in large "acidic" and small "basic" subunits linked by disulphide bonds. The large subunits of B species are more acidic and less heterogeneous than the corresponding subunits of the A species. These results confirm that helianthinin had a "legumin-type" structure.
采用二维电泳法研究了向日葵种子球蛋白组分的亚基异质性，第一维采用等电聚焦，第二维采用十二烷基硫酸钠聚丙烯酰胺凝胶电泳。在非还原条件下，中间亚基B、C和D（分子量分别为54000、48000和40000）聚焦在pH值范围5.4 - 6.0内，但中间亚基A（分子量60000）聚焦在pH值范围6.3 - 6.8内。在还原条件下，电泳图谱表明中间亚基由通过二硫键连接的大的“酸性”亚基和小的“碱性”亚基组成。B种的大亚基比A种的相应亚基酸性更强且异质性更小。这些结果证实了向日葵球蛋白具有“豆球蛋白型”结构。
