Abstract
Summary
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° for 30 min. does not contain these activities. The anti-complementary activity of AE is directed primarily against C'4; the esterase activity is demonstrable using TAMe and AcTyEe as substrates. Antigen-antibody aggregates adsorb C'1 or a factor closely resembling it, which upon elution appears to be identical to a previously described esterase derived from partially purified C'1. These results indicate that C'1 exists in serum as a proenzyme which is converted to an active esterase by antigen-antibody aggregates.
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