1. Michaelis Constants for Isolated Cholinesterase Systems
- Author
-
James G. Beasley and Samuel T. Christian
- Subjects
chemistry.chemical_classification ,Chromatography ,biology ,Kinetics ,Pharmaceutical Science ,Substrate (chemistry) ,In Vitro Techniques ,Acetylcholine ,Enzyme ,chemistry ,Human plasma ,Enzymatic hydrolysis ,biology.protein ,Acetylcholine Chloride ,Cholinesterases ,Humans ,Organic chemistry ,Cholinesterase - 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.
- Published
- 1968