Abstract
Several isozymes of acetylcholinesterase are separated by 10% acrylamide gel electrophoresis of mouse blood, brain, heart, muscle and tongue tissues. Two isozymes migrating near the origin are described which show changes in relative activity during development. The faster of the two bands is proportionately higher in concentration in embryonic tissues and is highly specific for the acetylthiocholine iodide substrate. This isozyme corresponds to the erythrocyte membrane AChE in electrophortic mobility and substrate specificity. The slower of the two bands is predominant in adult tissues and exhibits considerable cross reaction with the butyrylthiocholine iodide substrate. During embryonic and postnatal developmental stages there is a gradual shift from the faster migrating isozyme toward a predominance of the slower migrating isozyme.
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