Podack E R, Kolb W P, Müller-Eberhard H J
J Immunol. 1976 Feb;116(2):263-9.
Procedures for the isolation of the human complement proteins C6 and C7 have been described. These procedures allow isolation of the two proteins without any loss of hemolytic activity. Apparent activity gains of 160% and 140% were observed for C6 and C7, respectively, when the activity of the isolated proteins was compared with their activity in serum. The recovery of C6 was 3.5 to 11% and that of C7 was 7 to 13% of the amount present in serum. C6 has a m.w.of 128,000 and an electrophoretic mobility at pH 8.6 of -2.6 times 10(-5) cm2 s-1 v-1. C7 has a m.w. of 121,000 and an identical electrophoretic mobility. With 3 times 10(7) assay cells, 63% hemolysis was achieved with 1 ng of C6 and 3.8 ng C7. On polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate and after reduction with mercaptoethanol, C6 and C7 behaved as single polypeptide chain proteins.
已描述了分离人补体蛋白C6和C7的方法。这些方法能够分离出这两种蛋白，且溶血活性无任何损失。当将分离出的蛋白活性与其在血清中的活性进行比较时，分别观察到C6和C7的表观活性增加了160%和140%。C6的回收率为血清中含量的3.5%至11%，C7的回收率为血清中含量的7%至13%。C6的分子量为128,000，在pH 8.6时的电泳迁移率为-2.6×10(-5) cm2 s-1 v-1。C7的分子量为121,000，电泳迁移率相同。使用3×10(7)个测定细胞，1 ng C6和3.8 ng C7可实现63%的溶血。在十二烷基硫酸钠存在下并经巯基乙醇还原后进行聚丙烯酰胺凝胶电泳时，C6和C7表现为单条多肽链蛋白。
