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Besançon, France

Andre C.,University of Franche Comte | Andre C.,Nanomedecine Laboratory | Herlem G.,University of Franche Comte | Herlem G.,Nanomedecine Laboratory | And 5 more authors.
Journal of Pharmaceutical and Biomedical Analysis | Year: 2011

This work was dedicated to the development of a new micro immobilized enzyme reactor (IMER) by using an in situ procedure. Arginase was covalently immobilized on an ethylenediamine (EDA) monolithic convective interaction media (CIM) disk (12. mm × 3. mm i.d.) previously derivatized with glutaraldehyde. The activity of this IMER was investigated by inserting this micro-IMER in a HPLC system. The effect of the arginase inhibitors was evaluated by the simultaneous injection of each inhibitor with the nitro guanidino benzene (NGB) substrate. The relative IC50 values were found in agreement with those derived by the conventional spectrometric method. This arginase micro-IMER system was also used to study the effects of plant-derived products on the arginase activity. The pet ether extract from the stem bark of the plant Ficus glomerata Roxob. and the procyanidin oligomers of cocoa and chocolate inhibit the arginase activity. Our results confirmed the direct effect of some plant extracts on the arginase activity and their interest in therapies for treating several NO-dependent smooth disorders. © 2011 Elsevier B.V. Source

Andre C.,University of Franche Comte | Andre C.,Nanomedecine Laboratory | Aljhani R.,University of Franche Comte | Aljhani R.,Nanomedecine Laboratory | And 4 more authors.
Journal of Separation Science | Year: 2011

The retention mechanism of a series of peptides on a single-wall carbon nanotube (SWCNT) stationary phase inside an HPLC column was investigated over a wide range of mobile phase compositions. While the similar size C18 column exhibited an efficiency of 11.5 μm, the SWCNT column increased the efficiency, i.e. 7.10 μm at a flow rate of 0.8 mL/min, and significantly affected the separation quality of the peptides. The values of enthalpy (δH) and entropy (δS) of transfer of the peptides from the mobile to the SWCNT stationary phase were determined. The method studied each factor, i.e. ACN fraction x in the ACN/water mixture and column temperature. The changes in retention factor, δH and δS as a function of the ACN fraction in the mobile phase were examined. These variations are explained using the organization of ACN in clusters in the ACN/water mixture and on the steric and electronic forces implied in the retention process. The information obtained in this work makes this SWCNT stationary phase useful for peptide research and demonstrated the role of ACN to improve the separation quality. © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. Source

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