10.30684/ etj.29.4.2


This work addresses the kinetic analysis of the interaction of some
oxadiazoles (L1 , L2, L3 & L4) in ethanol with serum acetylcholinesterase. It was
found that ethanol have inhibitory effect (25.18%) on AChE enzyme for this
reason niglicable it as solvent and instead of it use dimethyl sulfoxide which had
no effect. The % inhibition of L1 , L2, L3 & L4 at 10-7 M was
45.42,71.51,54.67&74.27 respectively and it elevated with increasing the
concentration till at 10-1 M it reached 53.62,99.08,56.22&99.43 respectively. The
effect of both L2 & L4 was reversible in nature. Michaelis – Menten constant and
maximum velocity for the hydrolysis of acetyl thiocholine iodide by AChE were
determined in control and treated systems. Line weaver – Burk plot and
their secondary replots indicated that the nature of inhibition in both compounds
was noncompetitive inhibition. The value of Ki was estimated also. The
mechanism of action of these types of compounds acting as inhibitors to the AChE
is suggested.