Bock H G, Skene P, Fleischer S, Cassidy P, Harshman S
Science. 1976 Jan 30;191(4225):380-3. doi: 10.1126/science.1859.
Chromatography on controlled pore glass in combination with chaotropic buffers makes possible, in a single step, protein purifications of several hundredfold. The new emphasis is on highly selective controllable adsorption. The method is useful for the purification and concentration of proteins from large volumes of complex media and for the purification of proteins that are poorly soluble or tend to aggregate in aqueous solution D-(-)-Beta-Hydroxybutyrate dehydrogenase, a mitochondrial membrane-bound protein, several soluble proteins, and staphylococcal alpha toxin, which can be purified directly from large volumes of culture medium, are used to illustrate the method.
在可控孔径玻璃上进行色谱分离并结合离液序列高的缓冲液，能够一步实现几百倍的蛋白质纯化。新的重点在于高度选择性的可控吸附。该方法可用于从大量复杂培养基中纯化和浓缩蛋白质，以及纯化在水溶液中溶解性差或易于聚集的蛋白质。D-(-)-β-羟基丁酸脱氢酶（一种线粒体膜结合蛋白）、几种可溶性蛋白以及可直接从大量培养基中纯化的葡萄球菌α毒素，都被用于说明该方法。
