Miribel L, Arnaud P
Department of Microbiology and Immunology, Medical University of South Carolina, Charleston 29425.
J Chromatogr. 1987 Sep 18;405:337-45. doi: 10.1016/s0021-9673(01)81775-1.
Alpha 1-beta glycoprotein (A1B) was purified to homogeneity from human plasma using a three-step procedure involving pseudo-ligand affinity chromatography on immobilized Cibacron Blue 3-GA, gel filtration chromatography on Sephadex G-200 and ion-exchange chromatography on DEAE Affigel Blue. The overall yield of the combined techniques was 31%. The major advantages of this technique include its conveniency, and the fact that no apparent alteration of the purified protein occurred as judged by the absence of modification of its physicochemical parameters. A1B appears to be present in normal plasma as a major form of Mr 70,000 daltons with extensive charge heterogeneity, together with minor components of higher Mr.
使用三步法从人血浆中纯化出均一的α1-β糖蛋白（A1B），该方法包括在固定化的汽巴蓝3-GA上进行假配体亲和色谱、在Sephadex G-200上进行凝胶过滤色谱以及在DEAE Affigel Blue上进行离子交换色谱。这些组合技术的总产率为31%。该技术的主要优点包括其便利性，以及从其理化参数未发生改变可判断纯化后的蛋白质未出现明显变化这一事实。A1B在正常血浆中似乎以分子量为70,000道尔顿的主要形式存在，电荷异质性广泛，同时还有较高分子量的次要成分。
