Biochromatographic framework for analyzing magnesium chloride salt dependence on nor-NOHA binding to arginase enzyme

A new arginase enzymatic reactor: Development and application for the research of plant-derived inhibitors

“…Of interest, arginase was found to reciprocally regulate nitric oxide (NO) levels in endothelial cells by competing with NO synthase for the substrate l-arginine [8]. Recently our group demonstrated that arginase inhibition improves endothelial function and lowers blood pressure on spontaneously hypertensive rats [9,10] and the binding of arginase inhibitors with the enzyme using a novel biochromatographic column [11,12] was studied. In the present study arginase was for the first time covalently immobilized on an amine monolithic activated support obtained by reacting the native epoxy groups with a convenient ethylene diamine spacer.…”

Experimental studies of OH° radical/pressure dependence of arginase activity using a molecular chromatography approach

“…The ex vivo characterization of drug candidates on isolated target enzymes, unfortunately, is often associated with long, labor-intensive assays and a large amount of disposable expensive material. Our group recently developed a novel immobilized arginase reactor for the binding mechanism study of a series of arginase inhibitors with the enzyme and the magnesium effect on this association process [16,17]. This paper describes a novel procedure for studying both the direct role of OH • radical formation and pressure on the arginase activity.…”