| Budget Amount *help |
¥1,700,000 (Direct Cost: ¥1,700,000)
Fiscal Year 1987: ¥400,000 (Direct Cost: ¥400,000)
Fiscal Year 1986: ¥1,300,000 (Direct Cost: ¥1,300,000)
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| Research Abstract |
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.
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