Abstract

1. Starch gel electrophoresis of rat brain homogenates has demonstrated 9 esterases which hydrolyze α-naphthyl acetate and naphthol AS-acetate. One of these has been identified as acetylcholinesterase. The nature of the others is undefined. In addition an enzyme (presumably pseudocholinesterase) acting against butyrylthiocholine iodide has been located at the site of sample insertion. 2. Homogenates of human white matter have yielded 9 esterases active against the same naphthol substrates. None of these is a cholinesterase. However, with acetylthiocholine iodide as substrate, acetylcholinesterase is demonstrable in human material. Enzymic activity against butyrylthiocholine iodide is demonstrable at the origin in human material, also. 3. Best results are obtained by use of homogenates centrifuged at 20,000 x g for 60 minutes.

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