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.