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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Leytus, S. P. Bowles, L. K. Mangel, W. F. Konisky, J. |
| Abstract | Preparations of outer membrane of two strains of Escherichia coli contain a protease that can activate the serum zymogen plasminogen to the active protease plasmin. The amount of plasmin formed is proportional to the membrane concentration. The kinetics of plasminogen activation are linear and obey the Michaelis--Menten rate equation. The Km(app) for the activation of dog plasminogen by E. coli outer membrane preparations is similar to the Km(app) for the activation of dog plasminogen by human urokinase. The E. coli enzyme is active in a membrane-associated form, as opposed to a secreted or soluble form, and is most likely a serine protease because it is inhibited by diisopropyl fluorophosphate. It is also inhibited from activating plasminogen by p-nitrophenyl-p-guanidinobenzoate and aprotinin. Analysis of the activation of plasminogen by the E. coli enzyme by NaDodSO4/polyacrylamide gel electrophoresis showed that the cleavage of plasminogen to plasmin was as specific as that exhibited in the activation of plasminogen to plasmin by urokinase. Possible in vivo roles for this plasminogen activator in E. coli outer membranes are discussed. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 3 |
| Volume Number | 78 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 1981-07-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Escherichia Coli Enzymology Fibrinolysin Metabolism Peptide Hydrolases Plasminogen Cell Membrane Enzyme Activation Kinetics Streptokinase Urokinase-Type Plasminogen Activator Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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