An enzyme inhibition biosensor, developed in our laboratory and previously used for the analysis of compounds with anticholinesterase activity (e.g. physostigmine, neostigmine, pyridostigmine nicotine and organophosphorus compounds) has now been tested for the analysis of another recently synthesized cholinesterase inhibitor, i.e. eptastigmine. In addition nicotinic acid and nicotinamide, although displaying weaker inhibition properties, were also tested in pharmaceutical products using the same inhibition enzyme sensor. The biosensor consisted of a hydrogen peroxide amperometric electrode coupled to a functionalised nylon membrane chemically bonding both the enzymes butyrylcholinesterase and choline oxidase; a butyrylcholine standard solution in glycine buffer acted as substrate. The response of the system to all the inhibitors considered was characterised completely and the analysis of several pharmaceutical formulations containing nicotinamide or nicotinic acid was also performed.
An enzyme inhibition biosensor, developed in our laboratory and previously used for the analysis of compounds with anticholinesterase activity (e.g. physostigmine, neostigmine, pyridostigmine nicotine and organophosphorus compounds) has now been tested for the analysis of another recently synthesized cholinesterase inhibitor, i.e. eptastigmine. In addition nicotinic acid and nicotinamide, although displaying weaker inhibition properties, were also tested in pharmaceutical products using the same inhibition enzyme sensor. The biosensor consisted of a hydrogen peroxide amperometric electrode coupled to a functionalised nylon membrane chemically bonding both the enzymes butyrylcholinesterase and choline oxidase; a butyrylcholine standard solution in glycine buffer acted as substrate, The response of the system to all the inhibitors considered was characterised completely and the analysis of several pharmaceutical formulations containing nicotinamide or nicotinic acid was also performed.
Epstigmine, nicotinamide and nicotinic acid determination using an inhibition enzyme sensor: application to pharmaceutical analysis / Campanella, L; Cocco, R; Favero, G; Sammartino, Maria Pia; Tomassetti, M.. - In: ANNALI DI CHIMICA. - ISSN 0003-4592. - 92:4(2002), pp. 373-385. (Intervento presentato al convegno Conference on Third Millenium: The Future of Analytical Chemistry in the Control of Foods and the Environment tenutosi a ROME, ITALY nel FEB 22-24, 2001).
Epstigmine, nicotinamide and nicotinic acid determination using an inhibition enzyme sensor: application to pharmaceutical analysis
FAVERO G;SAMMARTINO, Maria Pia;
2002
Abstract
An enzyme inhibition biosensor, developed in our laboratory and previously used for the analysis of compounds with anticholinesterase activity (e.g. physostigmine, neostigmine, pyridostigmine nicotine and organophosphorus compounds) has now been tested for the analysis of another recently synthesized cholinesterase inhibitor, i.e. eptastigmine. In addition nicotinic acid and nicotinamide, although displaying weaker inhibition properties, were also tested in pharmaceutical products using the same inhibition enzyme sensor. The biosensor consisted of a hydrogen peroxide amperometric electrode coupled to a functionalised nylon membrane chemically bonding both the enzymes butyrylcholinesterase and choline oxidase; a butyrylcholine standard solution in glycine buffer acted as substrate. The response of the system to all the inhibitors considered was characterised completely and the analysis of several pharmaceutical formulations containing nicotinamide or nicotinic acid was also performed.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
