Eptastigmine,nicotinamide and nicotinic acid determination using an inhibition enzyme sensor; application to pharmaceutical analysis

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.     

Vortex Layers of Small Thickness

We consider a 2D vorticity configuration where vorticity is highly concentrated around a curve and exponentially decaying away from it: the intensity of the vorticity is O(1/ε) on the curve while it decays on an O(ε) distance from the curve itself. We prove that, if the initial datum is of vortex-layer type, Euler solutions preserve this structure for a time that does not depend on ε . Moreover, the motion of the center of the layer is well approximated by the Birkhoff-Rott equation. © 2020 Wiley Periodicals, Inc.     

Further development of catalase, tyrosinase and glucose oxidase based organic phase enzyme electrode response as a function of organic solvent properties

Using three enzyme sensors (tyrosinase, catalase and glucose oxidase), capable of functioning also in non-aqueous solvents, we found new correlations between classical indicators, e.g. the log P value of several organic solvents and new empirical indicators such as ;maximum current variation' (MCV) and above all the ;current variation rate' (CVR), the values of which may be monitored with the biosensor considered dipping directly into the organic solvent. The trend of the immobilised specific activity of the tyrosinase enzyme dipping into different organic solvents was evaluated and compared with that determined by the spectrophotometric method. Lastly, an investigation was performed to experimentally verify the relation between hydrophobicity of the solvent and its ability to draw back the water from the enzyme microenvironment using the Karl Fischer method and thermogravimetric analysis to estimate the residual water in the enzyme microenvironment after having treated the enzyme with the organic solvent, then allowing it to dry.     

A Note on the analytic solutions of the Camassa–Holm equation

In this Note we are concerned with the well-posedness of the Camassa–Holm equation in analytic function spaces. Using the Abstract Cauchy–Kowalewski Theorem we prove that the Camassa–Holm equation admits, locally in time, a unique analytic solution. Moreover, if the initial data is real analytic, belongs to $H^s(\mathbb{R})$ with $s>3/2$, $6u_0{6}_{L^1}<\infty$ and $u_0?u_{0xx}$ does not change sign, we prove that the solution stays analytic globally in time. To cite this article: M.C. Lombardo et al., C. R. Acad. Sci. Paris, Ser. I 341 (2005).     

Conservative methods for the Toda lattice equations

We are concerned with the numerical integration of the Todalattice equations by using different conservative methods. Numericalexperiments suggest that the global error for isospectral schemesdecreases exponentially with time but it is almost constantfor either symplectic or more general integrators. We providea theoretical explanation for these experimental findings.