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Variations in acetylcholinesterase from brain and muscle of a freshwater air-breathing teleost, Heteropneustes fossilis.

Specific staining on polyacrylamide gel of acetylcholinesterase (AchE) from brain and muscle of Heteropneustes fossilis showed one major tissue specific band in each. Eserine inhibited the enzyme competitively in both tissue homogenates. However, the normal level of activity and the pattern of the rate of inhibition with increasing eserine concentrations were different. Muscle showed higher AchE specific activity than brain. There was a hyperbolic increase in the percent of inhibition of AchE activity by eserine in muscle whereas in brain the pattern was biphasic. The apparent Km and Vmax in the two tissue homogenates were also different. The results suggest structural and functional variations of AchE in brain and muscle of H. fossilis.