Schwenke K D, Raab B, Linow K J, Pähtz W, Uhlig J
Nahrung. 1981;25(3):271-80. doi: 10.1002/food.19810250307.
An isolation procedure for the 12 S rapeseed globulin is described which includes precipitation by dialysis, purification using gel chromatography on Sephadex G-200, and ion-exchange chromatography on DEAE-Sephadex A-50. The isolated globulin represents a neutral protein with an isoelectric point at pH 7.25--determined by isoelectric focusing--and a relation of the acidic to basic amino acid residues (epsilon Glu, Asp--Amide ammonia: epsilon Arg, Lys, His) of 1.0. As in other storage globulins high contents of glutamic (19%) and aspartic (10%) acid and a low content of sulphur containing amino acids are characteristic for the amino acid composition. Amongst the basic amino acids arginine has the highest percentage (7%). Opposite to results of other authors the sugar content of the globulin is low (0.5%). From the amino acid composition an average hydrophobicity according to Bigelow was calculated which amounts to be 1041 cal/res. (4.36 kJ/res.).
本文描述了一种12S油菜籽球蛋白的分离方法，该方法包括透析沉淀、使用Sephadex G - 200凝胶色谱纯化以及DEAE - Sephadex A - 50离子交换色谱。通过等电聚焦测定，分离得到的球蛋白是一种中性蛋白质，其等电点为pH 7.25，酸性与碱性氨基酸残基（ε-谷氨酸、天冬氨酸 - 酰胺氨：ε-精氨酸、赖氨酸、组氨酸）的比例为1.0。与其他储存球蛋白一样，氨基酸组成的特征是谷氨酸（19%）和天冬氨酸（10%）含量高，含硫氨基酸含量低。在碱性氨基酸中，精氨酸的百分比最高（7%）。与其他作者的结果相反，该球蛋白的糖含量较低（0.5%）。根据比奇洛方法从氨基酸组成计算出平均疏水性为1041卡/残基（4.36千焦/残基）。
