Detremination of kinetic effect of Metoprolol and Ranitidine on HRP- modified GC electrode biosensor
Peroxidase is classified as oxido reductive enzyme which catalyzes the oxidation of the substrate by a hydrogen peroxide solution, the composition of a protein which is the prosthetic group of HEM. Inthispaper,the effect of active substance from the diffe
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stract. Peroxidase is classified as oxidoreductive enzyme which catalyzes the oxidation of the substrate by a hydrogen peroxide solution, the composition of a protein which is the prosthetic group of HEM. In this paper, the effect of active substance from the different groups of drugs on peroxidase activity was studied. Electrochemical tests were performed in classical three – electrode system with techniques of cyclic voltametry and chronoamperometry. Amperometric biosensor for the determination of H2O2 is presented, based on GC electrode on which peroxidase is immobilized in Nafion film. Cyclic voltametry technique was used to research the influence of different substrate concentration on the enzyme activity in a potential range between – 1,0 V and 0,7 V and scan rate of 50 mV/s. Chronoamperometric technique was used for the determination of kinetic parameters Km and Vmax at a constant potential of 0,9 V.
Introduction Medicine in twenty- first century has largely become a molecular science in which drug molecules are directed toward specific macromolecular targets whose bioactivity is pathogenic or at least associated with disease. In most clinical situations the most desirable course of treatments is by oral administration of safe and efective drugs with a duration of action that allows for convenient dosing schedules (typically once or twice a day). These criteria are best met by small molecule drugs, as opposed to peptide, protein, gene, or many natural product – based therapeutics. Among the biological macromolecules that one can envisage as drug targets, enzymes hold a preeminent position because of the essentiality of their activity in many disease processes and because the structural determinants of enzyme catalisys lend themselves well to inhibition by small molecular weight, drug – like molecules. [1]. Not suprisingly, enzyme inhibitors represent almost half the drugs in clinical use today. It is therefore certain that specif© Springer Nature Singapore Pte Ltd. 2017 A. Badnjevic (ed.), CMBEBIH 2017, IFMBE Proceedings 62, DOI: 10.1007/978-981-10-4166-2_63
ic enzyme inhibition will remain a major focus of pharmaceutical research for the forseeable future [2]. Although enzymes are essential for life, dysregulated enzyme activity can also lead to disease states. In some cases mutations in genes encoding enzymes can lead to abnormally high concentrations of the enzyme within a cell (overexpression). Alternatively, point mutations can lead to an enhancement of the specific activity (i.e., catalytic efficiency) of the enzyme because of structural changes in the catalytically critical amino acid residues. By either of these mechanisms, aberrant levels of the reaction product’s formation can result, leading to specific pathologies so human enzymes, especially oxidoreductases (e.g. peroxidase, catalase...) are also commonly targeted for pharmacological intervention in many diseases. Enzymes, then, are attractive targets for drug therapy because of their essential roles in life processes and in pathophysiology. Ind
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