The interaction of the 56-kilodalton (kDa) proteinase from Serratia marcescens with human plasma activated C1 (C1̄) inhibitor, α2-antiplasmin, and antithrombin III was investigated. The 56-kDa proteinase was not affected by these inhibitors; on the contrary, all the inhibitors were inactivated by the 56-kDa proteinase within 2 to 6 h. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicated that all three inhibitors showed decreased in molecular weight of approximately 8,000 to 10,000 as a result of proteolytic cleavage by the 56-kDa proteinase. The 56-kDa proteinase also inactivated serum complement within 2 to 6 h. The loss of inhibitory activity caused by the 56-kDa proteinase, together with the effects of endogenous serine proteinases, may facilitate tissue destruction and inflammation.
|Number of pages||4|
|Journal||Infection and immunity|
|Publication status||Published - 1989 Jan 1|
ASJC Scopus subject areas
- Infectious Diseases