Fischetti V A, Gotschlich E C, Siviglia G, Zabriskie J B
J Exp Med. 1976 Jul 1;144(1):32-53. doi: 10.1084/jem.144.1.32.
Group A streptococcal M protein was extracted with nonionic detergent and subjected to a number of physical, chemical, and immunological tests. M protein thus extracted was composed of multiple protein bands, ranging from 35,000 down to 6,000 daltons, all having type-specific precipitating activity. The anti-phagocytic proteins, however, were limited to three molecular species having mol wt of 28,000, 31,000, and 35,000 daltons, and could be separated from those proteins that had only type specificity. Physical studies indicated that these proteins existed as individual asymmetrical molecules which were not aggregated. By radiolabeling M protein on living streptococci, it was determined that these protein bands were found on the streptococcal cell wall in this multiple form. Also, by pulse chase experiments supported by chemical and immunological data, evidence was obtained strongly suggesting that the smaller, type-specific molecules are used to assemble the larger, antiphagocytic proteins.
用非离子去污剂提取A组链球菌M蛋白，并对其进行了多项物理、化学和免疫学测试。如此提取的M蛋白由多条蛋白带组成，分子量从35,000道尔顿到6,000道尔顿不等，均具有型特异性沉淀活性。然而，抗吞噬蛋白仅限于分子量为28,000、31,000和35,000道尔顿的三种分子类型，并且可以与仅具有型特异性的那些蛋白分离。物理研究表明，这些蛋白以不聚集的单个不对称分子形式存在。通过对活链球菌上的M蛋白进行放射性标记，确定这些蛋白带以这种多种形式存在于链球菌细胞壁上。此外，通过化学和免疫学数据支持的脉冲追踪实验，有力地获得了证据，表明较小的型特异性分子用于组装较大的抗吞噬蛋白。
