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Acetylcholinesterase (AChE) was isolated from rat cerebral cortex and from rat retina. AChE was purified to homogeneity using ammonium sulfate precipitation and DEAE-Sephadex ion-exchange chromatography. The enzyme was purified 192-fold from the cortex and 199-fold from the retina. In terms of specific activity the enzyme was 30 times more active in the cortex and 20 times more active in the retina. Similar characteristics were found for brain AChE. The enzyme was found to be relatively stable against p-nitrophenyl acetate hydrolysis. Between 10 degrees C and 25 degrees C inactivation of enzyme activity in the cortex and in the retina was 4.3% and 3.5%, respectively, per year. When the brain was perfused with a medium containing glutathione (GSH), protection of brain AChE against inactivation was observed. This protection was related to the concentration of GSH in the perfusion medium and was probably due to a reaction between AChE and GSH. The molecular weight of the enzyme was found to be similar to other mammalian AChE./*
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import static java.lang.annotation.ElementType.FIELD;
import static java.lang.annotation.ElementType.METHOD