Kinetic Determination of Drug Particles Concentration via Enzyme-Catalyzed Decomposition of Hydrogen Peroxide

The inhibition effect of blood pressure control drug particles, metoprolol (C 34 H 56 N 2 O 12 ), and atenolol (C 14 H 22 N 2 O 3 ), on the enzyme catalyzed decomposition of hydrogen peroxide reaction has been investigated by ultraviolet spectrophotometry. The results obtained when hydrogen peroxide...

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Bibliographic Details
Published in:Particulate science and technology 2011-11, Vol.29 (6), p.493-502
Main Authors: Pogacean, F., Baldea, I., Olenic, L., Pruneanu, S., Biris, A. S.
Format: Article
Language:English
Subjects:
atenolol
Blood pressure
catalase
Chemical reactions
Corrosion inhibitors
Drugs
Enzyme kinetics
Hydrogen peroxide
hydrogen peroxide decomposition
Inhibition
inhibition mechanism
metoprolol
Prescription drugs
Reaction kinetics
Spectrophotometry
Spectrum analysis
Stoichiometry
UV spectrophotometry
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Summary:The inhibition effect of blood pressure control drug particles, metoprolol (C 34 H 56 N 2 O 12 ), and atenolol (C 14 H 22 N 2 O 3 ), on the enzyme catalyzed decomposition of hydrogen peroxide reaction has been investigated by ultraviolet spectrophotometry. The results obtained when hydrogen peroxide was spectrophotometrically monitored were compared with those previously obtained from electrochemical measurements. As expected, the two series of measurements were shown to be consistent with the reaction stoichiometry. The Lineweaver-Burk linear equation was used to determine the Michaelis-Menten constant (K M ) and the maximum reaction rate (r max ). Based on the variation of the Michaelis-Menten constant, respectively, the maximum reaction rate with inhibitor concentration, it was determined the inhibition parameters that characterize the enzyme-inhibitor (EI) and the enzyme-inhibitor-substrate (EIS) complexes. A mixed inhibition mechanism has been established for both drugs. Due to its selectivity and sensitivity, the development of a kinetic method for trace analysis of drugs, based on their inhibition effect on the enzyme-catalyzed reaction rate appears to be promising.
ISSN:0272-6351
1548-0046
DOI:10.1080/02726351.2010.521234