Abstract
SummaryConcentrations of human C'1 esterase which are below threshold for direct enhancement of vascular permeability in guinea pig skin have been shown capable of generating a partially heat stable (56†C, 30 minutes) permeability factor from normal guinea pig serum in vitro. The action of this factor was blocked by treatment of test animals with an anti-histaminic drug, tripolidine. Generation of the factor from serum was prevented by inactivation of the enzymatic activity of C'l esterase with DFP or human serum inhibitor of C'l esterase. SBTI, without effect on C'l esterase, did not inhibit generation. Concentrations of C'l esterase which elaborated permeability activity in guinea pig serum also produced marked depression of the hemolytic complement titer of the serum. A relationship was also observed between the residual complement titers of heated sera and their capacity to produce a permeability factor upon mixture with C'l esterase. The data are consistent with, but do not prove, the hypothesis that...
Published Version
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Schedule a callMore From: Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.)
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