Abstract
The enzymatic hydrolysis of acetylcholine chloride by human plasma cholinesterase has been studied in detail. Results suggest that at substrate concentrations below 0.01 M, Michaelis-Menten kinetics are followed and enzyme hydrolysis rates are due to a single enzyme component. At higher substrate concentrations, a second enzyme component appears to contribute significantly to the total velocity of the reaction and a Lineweaver-Burk plot yields a hyperbolic-type curve. Apparent Km values were calculated for the two components. The autohydrolysis rate for acetylcholine chloride at 26° was determined. The enzymatic hydrolysis of acetylcholine chloride by human plasma cholinesterase has been studied in detail. Results suggest that at substrate concentrations below 0.01 M, Michaelis-Menten kinetics are followed and enzyme hydrolysis rates are due to a single enzyme component. At higher substrate concentrations, a second enzyme component appears to contribute significantly to the total velocity of the reaction and a Lineweaver-Burk plot yields a hyperbolic-type curve. Apparent Km values were calculated for the two components. The autohydrolysis rate for acetylcholine chloride at 26° was determined.
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