Ghosh S K, Mukhopadhyay N K, Majumder S, Bose S K
Biochem J. 1983 Dec 1;215(3):539-43. doi: 10.1042/bj2150539.
The mycobacillin-synthesizing enzyme system was highly purified by fractionation at 30-55% (NH4)2SO4 saturation. The enzyme concentrate on Sephadex G-200 gel chromatography was resolved into three distinct fragments. Each of the fragments on further purification by DEAE-cellulose ion-exchange chromatography behaved as a single-component system, as clearly indicated by the sharpness of the peaks in the elution diagram. None of the fragments alone nor any two of them in all possible combinations possessed mycobacillin-synthesizing activity, which was restored only when the three fragments were used together in the test system.
通过在30 - 55%硫酸铵饱和度下分级分离，对合成分枝杆菌素的酶系统进行了高度纯化。在Sephadex G - 200凝胶色谱上的酶浓缩物被分离成三个不同的片段。通过DEAE - 纤维素离子交换色谱进一步纯化后，每个片段都表现为单一组分系统，洗脱图中的峰的尖锐程度清楚地表明了这一点。单独的任何一个片段，或者它们所有可能组合中的任意两个片段都不具有合成分枝杆菌素的活性，只有当这三个片段一起用于测试系统时，活性才得以恢复。
