INTERACTION OF CARBARYL WITH ACETYLCHOLINESTERASE OF THE TELEOST, CLARIAS-BATRACHUS

Acetylcholinesterase (AChE, EC 3.1.1.7) of Clarias Batrachus, a fresh water teleost, was localised both in the particulate and soluble fract ions of cell-free homogenate of the fish tissues. The particulate boun d enzyme could be solubilised using buffer containing Triton X-100 res ulting in maximum recovery of enzyme (88-92%) in the supernatant. Carb aryl at sublethal concentrations exerted an inhibitory effect on the l evel of AChE activity in the tissues of the fish. The inhibition was m ore pronounced when the fish was exposed with the subacute concentrati ons of the pesticide (1, 2 and 6 mg/l) for 15 days than for 96 hr. The re was much less difference between the inhibitory effects of carbaryl at 2 and 6 mg/l concentrations for both treatment durations, except i n gills where the inhibition was enhanced at increased concentration ( 6 mg/l). The interaction of carbaryl caused more inhibition of AChE ac tivity in brain and gills than liver and muscle of C. batrachus.