TAILIEUCHUNG - Báo cáo khoa học: Suppressed catalytic efficiency of plasmin in the presence of long-chain fatty acids Identification of kinetic parameters from continuous enzymatic assay with Monte Carlo simulation

Thrombi, which are dissolved primarily by plasmin (EC .), contain up to millimolar concentrations of fatty acids and these are known to affect the action of the protease. In the present study the modulation of plasmin activity was characterized quantitatively in a continuous amidolytic assay based on synthetic plasmin substrate (Spectrozyme-PL). | ễFEBS Journal Suppressed catalytic efficiency of plasmin in the presence of long-chain fatty acids Identification of kinetic parameters from continuous enzymatic assay with Monte Carlo simulation Anna Tanka-Salamon1 Kiril Tenekedjiev2 Raymund Machovich1 and Krasimir Kolev1 1 Department of MedicalBiochemistry Semmelweis University Budapest Hungary 2 Department of Economics and Management TechnicalUniversity Varna Bulgaria OnlineOpen Thisarticleis available free online at Keywords arachidonate Monte Carlo simulation oleate progress curves stearate Correspondence K. Kolev Department of Medical Biochemistry Semmelweis University Puskin u. 9 Budapest 1088 Hungary Fax 36 1 2670031 Tel 36 1 2661030 E-mail kale@ Website http Re-use of this article is permitted in accordance with the Creative Commons Deed Attribution which does not permit commercial exploitation Received 5 October 2007 revised 9 January 2008 accepted 14 January 2008 doi Thrombi which are dissolved primarily by plasmin EC . contain up to millimolar concentrations of fatty acids and these are known to affect the action of the protease. In the present study the modulation of plasmin activity was characterized quantitatively in a continuous amidolytic assay based on synthetic plasmin substrate Spectrozyme-PL . A novel numerical procedure was applied for identification of kinetic parameters and their confidence intervals with Monte Carlo simulation of the reaction progress curves providing adequate grounds for discrimination of different models of the enzyme action. All three fatty acids caused a 10-20-fold increase in the Michaelis constant on Spectrozyme-PL baseline value pM . The catalytic constant decreased from 1 to 1 in the presence of arachidonate and oleate but increased to 1 in the presence of stearate implying enhancement of plasmin activity at saturating substrate .

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