Isolation of the first component (C1) and the second component (C2) of carp complement

经6步纯化，从鲤鱼血清中分离到补体第一组分（C1）。从300 ml鲤鱼血清中提取鲤鱼氯约2.8 mg。最终制备的Cl溶血活性为初始Cl溶血活性的18%，血清蛋白含量为0.023%，纯化率为788倍。用抗全鱼血清（兔）免疫电泳法确定了分离的鲤鱼Cl的高纯度。鲤鱼C1的分子量估计为1020,000。EDTA处理对鲤鱼C1的溶血活性有抑制作用，但这种抑制作用可通过含Ca^<2+>缓冲液的透析来克服。加热（50℃，15 min）或与角叉菜胶孵育会破坏鲤鱼C1的溶血活性，但与氨、肼或酶聚糖孵育时仍能保持溶血活性。这些结果表明鲤鱼C1在化学性质上与哺乳动物C1相似。通过将eac1,4 （Yano et al., 1986）与缺乏C3的经肼处理的鲤鱼血清（Hd）在Mg^<2+>存在下孵育，制备了中间复合物eac1,4,2。EAC1、4、2和EAC1、4在不同灭活血清中表现出差异。也证实了EAC1、4、2和C3之间的反应不含二价阳离子。作者目前正努力从鲤鱼血清中分离C2。数据将于近期公布。

The first component of complement(C1) was isolated from carp serum by a 6-step purification procedure. About 2.8 mg of carp Cl was obtained from 300 ml of carp serum. The final preparatin contained 18% of the initial Cl hemolytic activity and 0.023% of the initial serum prote in, representing 788-fold purification. The high purity of the isolated carp Cl was established by immunoelectrophoresis against anti-whole carp serum (rabbit). The molecular weight of carp C1 was estimated to be 1,020,000. The hemolytic activity of carp C1 was inhibited by EDTA treatment, but this inhibition was overcome by dialysis against a Ca^<2+>-containing buffer. The hemolytic activity of carp C1 was destroyed by heating (50 C, 15 min) or incubation with carrageenan, but was retained when incubated with ammonia, hydrazine or zymosan. These results indicate that carp C1 resembles mammalian C1 in its chemical properties. An intermediate complex EAC1,4,2 was prepared by incubating EAC1,4 (Yano et al., 1986) with hydrazine treated carp serum (Hd), which is deficient in C3, in the presence of Mg^<2+>. The difference between EAC1,4,2 and EAC1,4 was shown by the tests with various inactivated sera. It was also confirmed that the reaction between EAC1,4,2 and C3 proceeds without any divalent cation. The author is now making efforts to isolate C2 from carp serum. Data will be published in the near future.