Schmidt K H, Köhler W
Zentralbl Bakteriol Mikrobiol Hyg A. 1984 Dec;258(4):449-56. doi: 10.1016/s0176-6724(84)80021-8.
T-protein of Streptococcus pyogenes, type 1 (strain SF 130 Griffith) was extracted by enzymatic treatment of the cells with trypsin and partially purified by ion exchange chromatography on DEAE cellulose and gel chromatography on ultrogel ACA 44. The crude T protein still showing serologically type specific and cross reactions finally was applied to a fibrinogen sepharose column. Components eluted with the neutral buffer (0.05 M phosphate, 0.2 M NaCl, 0.02% NaN3, pH 7.0) reacted serologically in the same manner as the crude T protein. By using 0.1 M citrate, 6 M urea pH 3.0 buffer a type specifically reacting protein (T1-TRYP-F) was eluted from the fibrinogen column. T1-TRYP-F showed identical precipitation lines with the recently characterized T1-protein (T1-TRYP-I) purified by immunochromatography on type specific anti-T antibodies. Comparison of the SDS-patterns of T1-TRYP-F and T1-TRYP-I revealed a less complex molecular size subunit structure for the fibrinogen binding T1-TRYP-F (two bands of 60000 and 70000) as found for T1-TRYP-I, which showed serologically active peptides between 30000 to about 500000. It is discussed that T protein also may be linked covalently with fibrinogen receptors as it has been reported for M protein.
1型化脓性链球菌（菌株SF 130 Griffith）的T蛋白通过用胰蛋白酶对细胞进行酶处理来提取，并通过在DEAE纤维素上的离子交换色谱和在ultrogel ACA 44上的凝胶色谱进行部分纯化。最终仍显示血清学类型特异性和交叉反应的粗T蛋白应用于纤维蛋白原琼脂糖柱。用中性缓冲液（0.05M磷酸盐、0.2M氯化钠、0.02%叠氮化钠，pH 7.0）洗脱的组分在血清学上的反应方式与粗T蛋白相同。通过使用0.1M柠檬酸盐、6M尿素pH 3.0缓冲液，从纤维蛋白原柱上洗脱了一种类型特异性反应蛋白（T1-TRYP-F）。T1-TRYP-F与通过在类型特异性抗T抗体上进行免疫色谱纯化的最近鉴定的T1蛋白（T1-TRYP-I）显示出相同的沉淀线。T1-TRYP-F和T1-TRYP-I的SDS图谱比较显示，与T1-TRYP-I相比，纤维蛋白原结合T1-TRYP-F的分子大小亚基结构不太复杂（两条带分别为60000和70000），T1-TRYP-I在30000至约500000之间显示血清学活性肽。据报道M蛋白存在这种情况，因此讨论了T蛋白也可能与纤维蛋白原受体共价连接。
