Microcalorimetric studies on the non-competitive inhibition of bovine liver arginase

Abstract

Two methods, e.g. initial rate method and thermokinetic reduced extent method were presented for studies on non-competitive inhibition. Arginase-catalyzed the hydrolysis of L-arginine toL-ornithine and urea and the inhibition of this reaction by sodium fluoride were studied in the absence and presence of exogenous of Mn²⁺at 37°C in 40 mM sodium barbiturate-hydrochloric acid buffer solution (pH 7.4). Both methods were successively used to determine the values of K₁. The advances and disadvantages of each method were compared in this paper. Exogenous Mn²⁺ could result in more sensitivity of arginase to F^-1. Since the inhibition of arginase by F^-1 depends on the pH values of the reaction system and behave as a non-competitive inhibition, it probably due to its small volume and high electronic density allow it access to the activity site of the enzyme and replaces of µ-OH₂ (or µ-OH) as the bridge ligand with Mn(II, II) cluster. However, further studies are necessary to determine the modes of interaction of F^-1 with bovine liver arginase.