Abstract
Immune precipitate (Ippt) formed between egg albumin and rabbit IgG antibody activated both pathways of the human complement system. On incubation with diluted serum, Ippt combined with several factors in the serum to form a complex which acquired C3-and C5-cleaving activities. In serum chelated with ethyleneglycol tetraacetic acid (EGTA), C3- and C5-cleaving activities of properdin system enzymes were formed on Ippt. Kinetic studies on the formation and the decay of C3-and C5-cleaving enzymes on Ippt revealed that C3- and C5-cleaving activities were almost dependent on the properdin system enzymes. The experiments in which C3-cleaving activity formed on Ippt was inhibited by anti-properdin or anti-B but not by anti-C4 supported the above results. The participation of the classical pathway was considered to accelerate the assembly of the properdin system enzymes.
