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The amidolytic activities of papain and rat liver cathepsins B, H and L were strongly inhibited by high (HMM) and low (LMM) molecular mass kininogens from bovine, human and rat plasmas, and their Ki values were estimated to be in the order of 10(-10) - 10(-11)M for papain and 10(-8) - 10(-9)M for cathepsins. The derivatives of bovine kininogens, HMM kinin-free protein, HMM kinin- and fragment 1 X 2-free protein, and LMM kinin-free protein also showed strong inhibitory activity toward these thiol-proteinases. These results suggest that a reactive site which interacts with thiol-proteinases is contained in the heavy chain portion in kininogens.
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