Lange C F, Lee R, Merdinger E
J Bacteriol. 1969 Dec;100(3):1277-83. doi: 10.1128/jb.100.3.1277-1283.1969.
M protein was extracted from the cell walls of streptococci by use of both acidic and alkaline buffers. These extracts were further purified by ammonium sulfate fractionation and column chromatography. Both diethylaminoethyl and carboxymethyl celluloses were employed to cover the pH range of 3.0 to 9.0. All of the M proteins isolated were immunologically related, but their physical and chemical properties varied dependent upon the pH range of isolation. Each isolate appeared to be homogeneous on the basis of immunodiffusion analysis, electrophoretic mobility, and ultracentrifugal analysis, but their amino acid analyses differed slightly. Two factors were shared by all isolates: (i) they all reacted with type-specific antisera and (ii) each seemed to have l-lysine as a single N-terminal amino acid.
通过使用酸性和碱性缓冲液从链球菌细胞壁中提取M蛋白。这些提取物通过硫酸铵分级分离和柱色谱进一步纯化。使用二乙氨基乙基纤维素和羧甲基纤维素来覆盖3.0至9.0的pH范围。所有分离出的M蛋白在免疫上相关，但其物理和化学性质根据分离的pH范围而变化。根据免疫扩散分析、电泳迁移率和超速离心分析，每个分离物似乎都是均一的，但它们的氨基酸分析略有不同。所有分离物都有两个共同因素：（i）它们都与型特异性抗血清反应，（ii）每个似乎都以L-赖氨酸作为单一的N末端氨基酸。
