Active Fragment in Normal Plasma Predominant Role of Ci-Inhibitor

To define the factors responsible for the inactivation ofthe active fragment derived from Factor XII (Factor XIIf) in plasma, we studied the inactivation kinetics of Factor XIIf in various purified and plasma mixtures. We also analyzed the formation of '25I-Factor XIIf-inhibitor complexes by sodium dodecyl sulfate poly- acrylamide gel electrophoresis (SDS-PAGE). In purified systems, the bimolecular rate constants for the reactions ofFactor XIIfwith Cl-inhibitor, a2-antiplasmin, and an- tithrombin III were 18.5, 0.91, and 0.32 X 104 M-' min-, respectively. Furthermore, SDS-PAGE analysis revealed that 1:1 stoichiometric complexes were formed between 125I-Factor XIIf and each of these three inhibitors. In contrast, kinetic and SDS-PAGE studies indicated that Factor XIIf did not react with a1-antitrypsin or a2-mac-

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