Kinetics for the Inhibition of Serum Acetylthiocholin Esterase Activity by Some Prepared Phenobarbital Derivatives

Abstract

Kinetics for the Inhibition of Serum Acetylthiocholin Esterase Activity by Some Prepared Phenobarbital Derivatives This work addresses the kinetic analysis on the interaction of some prepared Phenobarbital derivatives (A, B, C and D) with human serum acetylcholinesterase. It was found that these compound (A, B and D) does have inhibitory effects at different concentrations (10-4, 10-6, 10-8,    10-10M), and were observed to have elevated inhibition with increasing concentrations(10-10 to 10-4M) of concentrations for both compounds A and B, elevated inhibition with decrease concentration from 10-4 to 10-10M for D. The effects of each A, B and D were reversible in nature. All of the results for C compound were neglected. Michaelis- Menten constant and maximum velocity for hydrolysis of acetylthiocholine iodide by AChE was determined in control and treated systems. Line weaver-Burk plot and their secondary replots indicated that the nature of inhibition was (competitive at concentration 10-4, non competitive at 10-10 for A), (non competitive at 10-4, competitive at 10-10 for B), (non competitive at 10-4, and uncompetitive at 10-10 for D) respectively. The value of ki was also estimated. The action mechanism of these types of compounds acting as inhibitors to the AChE is suggested.