Manwell C
Biochem J. 1977 Sep 1;165(3):487-95. doi: 10.1042/bj1650487.
Electrophoresis of 31 different proteins in commercially prepared polyacrylamide gradient gels, Gradipore, yields a linear relationship between a hypothetical limiting pore size (the reciprocal of a limiting gel concentration, GL) and the cube root of the mol.wt., over the range 13 500-9000 000. A regression analysis of these data reveals that 98.6% of all variability in 1/GL is explained by the molecular weight, and this degree of accuracy compares favourably with existing methods for the determination of molecular weight by retardation of mobility in polyacrylamide. This new procedure has the additional advantages that molecular-weight standards can be obtained from readily available body fluids or tissue extracts by localizing enzymes and other proteins by standard histochemical methods, and that the same electrophoretic system can be used in determining molecular weights as is used in routine surveys of populations for individual and species variation in protein heterogeneity.
在市售的聚丙烯酰胺梯度凝胶(Gradipore)中对31种不同蛋白质进行电泳,在13500 - 9000000的分子量范围内,假设的极限孔径(极限凝胶浓度GL的倒数)与分子量的立方根之间呈现线性关系。对这些数据的回归分析表明,1/GL中所有变异性的98.6%可由分子量解释,与现有的通过聚丙烯酰胺中迁移率延迟来测定分子量的方法相比,这种准确度相当不错。这种新方法还有其他优点,即分子量标准品可通过标准组织化学方法定位酶和其他蛋白质,从容易获得的体液或组织提取物中获得,并且在测定分子量时可使用与在人群蛋白质异质性个体和物种变异的常规调查中相同的电泳系统。