SEPARATION AND PROPERTIES OF HUMAN BRAIN ESTERASES

Abstract

Concentrated super nates of saline homogenates of human brain were found by vertical starch gel electrophoresis to contain 20 to 25 water soluble proteins. At least 18 bands of enzymic activity against naphthyl esters were demonstrable by histochemical techniques. One of these had characteristics of a C-esterase. Protein and non-specific esterase patterns were similar in all brain regions examined. Thiocholine esters were hydrolyzed by 3 bands having properties of acetylcholinesterases. These did not hydrolyze non-choline esters. A distinct thioesterase was demonstrated. Certain bands, active against naphthol esters and thiolacetic acid, were capable of hydrolyzing a synthetic trypsin substrate.