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Regulation of fibrinolytic activity of neutrophil leukocyte elastase, plasmin, and miniplasmin by plasma protease inhibitors

Citation

Kolev, K and Lerant, I and Tenekedjiev, K and Machovich, R, Regulation of fibrinolytic activity of neutrophil leukocyte elastase, plasmin, and miniplasmin by plasma protease inhibitors, Journal of Biological Chemistry, 269, (25) pp. 17030-17034. ISSN 0021-9258 (1994) [Refereed Article]


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Copyright Statement

This research was originally published in the Journal of Biological Chemistry. Kolev, Krasimir and Lerant, Istvan and Tenekedjiev, Kiril and Machovich, Raymund. Regulation of fibrinolytic activity of neutrophil leukocyte elastase, plasmin, and miniplasmin by plasma protease inhibitors. J. Biol. Chem. 1994; Vol. 269, No. 25, pp. 17030-17034. 1994 the American Society for Biochemistry and Molecular Biology.

Official URL: http://www.jbc.org/content/269/25/17030.long

Abstract

The effect of solid-phase fibrin on the inactivation of plasmin, miniplasmin, and neutrophil leukocyte elastase (PMN-elastase) by plasma protease inhibitors (alpha 2-antiplasmin, alpha 1-protease inhibitor, alpha 2-macroglobulin) was studied. In Hanks' balanced salt solution, fibrin reduces the second-order rate constant for the inhibition of PMN-elastase by alpha 1-protease inhibitor from 8,760 x 10(4) to 4 x 10(4) M-1.s-1 and by alpha 2-macroglobulin from 121 x 10(4) to 1.8 x 10(4) M-1.s-1. The rate constant for miniplasmin inactivation by alpha 2-antiplasmin decreases from 99 x 10(4) to 1 x 10(4) M-1.s-1, by alpha 2-macroglobulin from 78 x 10(4) to 1.8 x 10(4) M-1.s-1, and by alpha 1-protease inhibitor from 0.11 x 10(4) M-1.s-1 to 0. Plasmin bound to fibrin is completely protected against alpha 2-macroglobulin and alpha 1-protease inhibitor, whereas the rate constant for the inactivation by its primary plasma inhibitor alpha 2-antiplasmin is reduced from 430 x 10(4) to 1.08 x 10(4) M-1.s-1. The competition of substrate and inhibitor for the enzyme was also studied, using fibrin preincubated with inhibitor. Under our pseudo-first-order experimental conditions, fibrin completely eliminates those interactions, the second-order rate constant of which is 1.1 x 10(5) M-1.s-1 or less in a system without fibrin surface.

Item Details

Item Type:Refereed Article
Keywords:enzyme kinetics
Research Division:Information and Computing Sciences
Research Group:Artificial intelligence
Research Field:Modelling and simulation
Objective Division:Expanding Knowledge
Objective Group:Expanding knowledge
Objective Field:Expanding knowledge in the information and computing sciences
UTAS Author:Tenekedjiev, K (Professor Kiril Tenekedjiev)
ID Code:127976
Year Published:1994
Web of Science® Times Cited:65
Deposited By:Governance Office
Deposited On:2018-08-26
Last Modified:2018-10-15
Downloads:22 View Download Statistics

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