LEV serum concentration-effect relationship has also been reported. Recently, Kauffman et al. reported a probable association of LEV dose or plasma concentrations to mood disorders. The therapeutic range of LEV has not been distinctly defined, but a trough level of between 12 and 46 mg/mL or between 70 and 270 mmol/mL was suggested. A number of laboratory methods such as immunoassay, high performance liquid chromatography with UV detection, gas chromatography with mass spectrometry detection, gas chromatography with nitrogen phosphorus detection, capillary electrophoresis with UV detection, high performance thin layer chromatography, high-performance liquid chromatography tandem mass spectrometry and ultra-performance liquid chromatography tandem mass spectrometry have been described for measuring LEV in biological matrices. Some of these assay methods however, may require large sample volumes, tedious extraction procedures using solid-phase extraction or liquid-liquid extraction or a lengthy chromatographic run time of 10 minutes or longer, for an analysis of a single analyte. LY2109761 Moreover, these assay methods mainly focus on the quantification of LEV, either alone or together with other antiepileptic drugs. Although it is not crucial to measure an inactive metabolite in a pharmacokinetic-pharmacodynamic study, a falsely higher measured LEV concentrations may result if LEV was not separated either chromatographically or mass spectrometrically from UCB L057 during a quantification process. Both compounds might co-elute as their molecular weights differ only by 1 mu and they also share a similar daughter ion of 126 mu which is often used for the quantification of LEV. To date, there is only one published assay method that measures the plasma concentrations of LEV and UCB L057 simultaneously by altering the pH of the mobile phase using a gradient elusion. Previous exploratory pharmacokinetic studies of LEV have employed two distinct analytical methods of GS-MS and LC-ESI-MS to quantify the plasma concentrations of LEV and UCB L057 respectively. The objective of this present work is to develop and validate a simple LC-MS/MS method for a simultaneous quantification of LEV and UCB L057 in the plasma of patients treated with LEV for seizure control in a population pharmacokinetic study. Plants use several strategies to overcome fungal attacks, including the production of antimicrobial peptides and proteins. Much effort has been dedicated to researching these bioactive constituents, particularly because the chemically-synthesized antifungal compounds used to prevent and contain these pathogens comprise a potential environmental threat. In general, these defense-related proteins interfere with the fungal life cycle by either impairing growth or killing the pathogen. The antifungal properties of these proteins may be exploited for use in the development of transgenic crops that have enhanced resistance to phytopathogenic fungi. Chitin-binding proteins represent a group of proteins also found in plants that often have a basic pI, a molecular mass ranging from 3.1 kDa up to 20 kDa, and high resistance to both extreme pH changes and proteolysis. Some CBPs have the ability to inhibit fungal growth, as they bind to and disrupt the proper function of chitin, a key component of the fungal cell wall. It has been suggested that the binding of these proteins to chitin in filamentous fungi leads to the disruption of both cell wall biogenesis and cell polarity. Recently, our research group isolated a chitin-binding protein named Mo-CBP3 from Moringa oleifera Lam. seeds.