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Direct Detection of the Acetate-forming Activity of the Enzyme Acetate Kinase
Published on: December 19, 2011
Kinetic method for acetylsalicylic acid determination based on its inhibitory effect upon the catalytic decomposition
Claudia Mureşanu1, Lucian Copolovici
1Faculty of Chemistry and Chemical Engineering, Babeş-Bolyai University, 11 Arany Janos Street, 3400, Cluj-Napoca, Romania. muresanu@ptc.tu-graz.ac.at
Abstract:
The catalytic reaction of catalase was investigated, by means of a Clark oxygen sensor, in the presence of various concentrations of acetylsalicylic acid. Michaelis-Menten kinetic parameters were determined from Lineweaver-Burk plots, obtained in the absence and in the presence of the inhibitor. The inhibition pattern, suggested by the Lineweave-Burk plots, corresponds to a fully mixed inhibition mechanism. A kinetic method, based on the indicator reaction: [Formula: see text], was developed for the quantitative determination of acetylsalicylic acid. Calibration graphs of the reciprocal value of first-order rate constant versus acetylsalicylic concentration covered the concentration range (2.99-19.98)x10(-4) mol/L, while the detection limit was 4.12x10(-4) mol/L acetylsalicylic acid with a standard deviation of 2.1x10(-5) mol/L.
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