Abstract
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.
Original language | English |
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Pages (from-to) | 1868-1871 |
Number of pages | 4 |
Journal | Infection and immunity |
Volume | 57 |
Issue number | 6 |
Publication status | Published - 1989 Jan 1 |
Externally published | Yes |
ASJC Scopus subject areas
- Parasitology
- Microbiology
- Immunology
- Infectious Diseases