Abstract
Summary C3 Inactivator (C3INA) purified from human serum has been measured by its ability to block the reactivity of the cellular intermediate EAC143 in immune hemolysis. Cells prepared with limited amounts of C3 are reacted with C3INA, resulting in the inactivation of a portion of this cell-bound C3. The residual active cell-bound C3 is then detected by a stoichiometric assay in which the remaining components are supplied in relative excess. The average number of SAC143 inactivated by C3INA is a function of C3INA input. The inactivation of cell-bound C3 by C3INA is time and temperature dependent, and the rate of the inactivation is related to the input of C3INA. During the inactivation of SAC143 by C3INA, C3b or a fragment thereof is released into the fluid phase. C3INA is not consumed during its interaction with cell-bound C3 suggesting that it is an enzyme. Human C3INA appears to be identical to the conglutinogen-activating factor described by Lachmann and Müller-Eberhard.
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