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Propranolol, a widely used beta-blocker, inhibits the reaction of enzyme  cholinesterase hydrolysis. Measurements of the hydrolysis rate differences  between and inhibited reactions, allows the development of a kinetic method  for its determination. Both systems, enzyme-substrate-chromogen and  enzyme-substrate-chromogen-inhibitor, were characterized through biochemical  kinetic parameters (KM = 0.326-0.330 mmol/L; Vmax = 40-42.99 μmol/Lmin),  inhibition type was recognized as competitive, and inhibition constant, Ki,  was determined to be 22.60 μmol/L. The detection and quantification limits  were calculated as 0.004 and 0.0136 μmol/L, respectively. Accuracy and  precision of proposed methods were tested. Proposed method is characterized  with good sensitivity, selectivity, simplicity and rapidity, thus it is  convenient for clinical applications

Enzymatic kinetic method for determination of propranolol hydrochloride in pharmaceuticals based on its inhibitory effect on cholinesterase