Havlícek J
Pathol Microbiol (Basel). 1975;42(3):147-58.
A method for the isolation and purification of M protein was developed. Purified cell walls were sonically disrupted, solubilized M protein was precipitated by ammonium sulphate and then electrofocused. Both in this material and in hot acid extracts type-specific trypsin-sensitive antigens with two separately precipitating moieties were found. Evidence is adduced showing that they both belong to the M protein complex. The molecular weight of our purified M protein ranged between 400,000 and 20,000 daltons, giving a peak at 150,000 daltons. The pI of this material was found to be 5.4-5.6. There were marked differences between the behaviour of the low, medium and high molecular weight fractions obtained from purified M protein by gel filtration.
开发了一种分离和纯化M蛋白的方法。将纯化的细胞壁进行超声破碎，用硫酸铵沉淀溶解的M蛋白，然后进行等电聚焦。在该材料和热酸提取物中均发现了具有两个分别沉淀部分的型特异性胰蛋白酶敏感抗原。有证据表明它们都属于M蛋白复合物。我们纯化的M蛋白的分子量在400,000至20,000道尔顿之间，在150,000道尔顿处出现峰值。发现该材料的pI为5.4 - 5.6。通过凝胶过滤从纯化的M蛋白获得的低、中和高分子量级分的行为存在明显差异。
