EFFECT OF MALATHION ON KINETIC-PARAMETERS OF ACETYLCHOLINESTERASE (EC-3.1.1.7) IN-VITRO

Kinetic analysis of the interaction of malathion with camel erythrocyt e acetylcholinesterase was investigated in the present study. The Mich aelis-Menten constant (K-m) for the hydrolysis of acetylthiocholine io dide (ASCh) was found to be 53.15 mu M and the V-max was 0.287 mu mol/ min/mg protein. The K-mapp and V-maxapp were both decreased by increas ed malathion concentration. Dixon as well as Lineweaver-Burk plots and their secondary replots indicated that the nature of the inhibition w as of the pure uncompetitive type with K-1 value estimated as 102.1 pp m. The K-iapp decreased while V-maxiapp increased by an increased conc entration in ASCh.