Kinetic Profiling of Phenobarbital Derivative Inhibition Levels on Serum Acetylthiocholine Esterase Activity

Abstract

This study uses human serum acetylcholinesterase to analyze the kinetics of a few produced phenolic derivatives (A, B, C, and D). The compounds A, B, and D were observed to exhibit inhibitory effects at varying concentrations (10-4, 10-6, 10-8, and 10-10 mM). Additionally, there was an increase in inhibition with increasing concentrations (10-10 to 10-4 mM) for compounds A and B and an increase in inhibition with decreasing concentrations (10-4 to 10-10 mM) for compound D. It was reversible how A, B, and D affected things. For the C compound, every result was disregarded. In both the treated and control systems, the Michaelis-Menten constant and maximum velocity for the hydrolysis of acetylthiocholine iodide by AChE were found. The supplementary replots for the line weaver-burk plot were shown.