Jacobs E, Fuchte K, Bredt W
Institut für Medizinische Mikrobiologie und Hygiene, Universität Freiburg.
Biol Chem Hoppe Seyler. 1988 Dec;369(12):1295-9. doi: 10.1515/bchm3.1988.369.2.1295.
The 168-kDa adherence protein of M. pneumoniae was solubilized and purified to homogeneity. Optimal yield was obtained by pretreatment of whole M. pneumoniae cells with buffer containing 1% Chaps and subsequent extraction with octylglucosid at a detergent to protein ratio of 5 and at octylglycoside concentrations between 1.5 and 2%. Contaminating membrane proteins with high molecular masses were removed by pretreatment with 1% Chaps and proteins of low molecular masses by size exclusion chromatography.
肺炎支原体的168 kDa黏附蛋白被溶解并纯化至同质状态。通过用含1% Chaps的缓冲液对肺炎支原体全细胞进行预处理，随后以去污剂与蛋白质比例为5且辛基葡糖苷浓度在1.5%至2%之间进行提取，可获得最佳产量。通过用1% Chaps预处理去除高分子量的污染膜蛋白，并通过尺寸排阻色谱法去除低分子量的蛋白。
