A new thermokinetic reduced extent method for studying of the reversible competitive inhibition of single sub-strate enzyme-catalyzed reactions was proposed in this paper. The reaction that arginase-catalyzed hydrolysis of L-arginine to L-ornithine and urea and the inhibition of this reaction by the product, L-ornithine, and exogenous L-lysine were studied at 37 ℃ in 40 mmolL-1 sodium barbiturate-HCl buffer solution (pH=9.4). Michealis con-stant Km for arginine and maximum velocity Vm of the reaction were determined to be 5.14 mmolL-1 and 1.13× 10-2 mmolL-1s-1, respectively. The product inhibition constant KP and inhibitory constant KI of L-lysine were de-termined to be 1.18 and 5.6 mmolL-1, respectively. All the results have better repeatability and self-consistency and are in agreement with literature values. This new method using more direct thermal information from the proc-ess would give more reliable kinetic information than the traditional initial rate method. A new thermokinetic reduced extent method for studying the reversible competitive inhibition of single sub-strate enzyme-catalyzed reactions was proposed in this paper. The reaction that arginase-catalyzed hydrolysis of L-arginine to L-ornithine and urea and the inhibition of this reaction by the product, L-ornithine, and exogenous L-lysine were studied at 37 ° C. in 40 mmol L -1 sodium barbiturate-HCl buffer solution (pH = 9.4). Michealis con-stant Km for arginine and maximum velocity Vm of the reaction were determined to be 5.14 mmol L-1 and 1.13 × 10 -2 mmol L-1 s-1, respectively. The product inhibition constant KP and inhibitory constant KI of L-lysine were de-termined to be 1.18 and 5.6 mmol L -1, respectively. All the results have better repeatability and self-consistency and are in agreement with literature values. This new method using more direct thermal information from the proc-ess would give more reliable kinetic information than the traditional initial rate method.