Elution of an Esterase from Antigen-Antibody Aggregates Treated with Human Complement.

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Abstract
An eluate (AE) prepared from antigen-antibody aggregates previously treated with fresh human serum contains esterase and anti-complementary activities. A corresponding eluate (UE) prepared from aggregates treated with serum heated at 56 [degree] for 30 minutes does not contain these activities. The anti-complementary activity of AE is directed primarily against C[image]4; the esterase activity is demonstrable using p-toluenesulfonyl-L-arginine methyl ester (TAMe) and acetyl-L-tyrosine ethyl ester (AcTYEe) as substrates. Antigen-antibody aggregates adsorb C[image]l or a factor closely resembling it, which upon elution appears identical to a previously described esterase derived from partially purified C[image]l. These results indicate that C[image]l exists in serum as a proenzyme which is converted to an active esterase by antigen-antibody aggregates.