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

C. André (1) , F. Ibrahim , T. Gharbi (2) , G. Herlem (2) , Y.-C. Guillaume (1)

1 FDE - Fonctions et dysfonctions épithéliales - UFC (EA 4267)
2 FEMTO-ST - Franche-Comté Électronique Mécanique, Thermique et Optique - Sciences et Technologies (UMR 6174)

Arginase is an enzyme which plays a role in pathophysiology such as hypertension. Here we demonstrated for the first time the direct implication of pressure and OH degrees radical formation on the arginase activity via a novel analytical procedure. Pressure increased arginase activity in the range 12-52 bars. Activation by OH degrees radical showed a hyperbolic response. The OH degrees radicals produced were significantly inhibited by sulfasalazine (SAZ) and the inhibition of OH degrees radicals parallels the inhibition of arginase activity.

Domaines: Optique / photonique

C. André, F. Ibrahim, T. Gharbi, G. Herlem, Y.-C. Guillaume. Experimental studies of OH degrees radical/pressure dependence of arginase activity using a molecular chromatography approach. Journal of Chromatography B - Analytical Technologies in the Biomedical and Life Sciences, 2010, 878 (28), pp.2826-2830. ⟨10.1016/j.jchromb.2010.08.036⟩. ⟨hal-00583377⟩