Premium
PURIFICATION AND PROPERTIES OF BRAIN ACETYL‐CHOLINESTERASE (EC 3.1.1.7) 1
Author(s) -
Chan S. L.,
Shirachi D. Y.,
Trevor A. J.
Publication year - 1972
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1972.tb01353.x
Subject(s) - acetylthiocholine , acetylcholinesterase , chemistry , chromatography , homogenization (climate) , centrifugation , molecular mass , hydrolysis , aché , electrophoresis , sucrose , specific activity , cholinesterase , enzyme , biochemistry , biology , biodiversity , ecology , pharmacology
— Approximately 50 per cent of the total AChE of brain tissue was solubilized by a simple procedure of repeated homogenization and centrifugation in 0.32 M‐sucrose containing EDTA. Ion‐exchange and molecular‐sieve chromatography demonstrated two peaks of AChE activity which apparently differed with respect to charge properties and molecular size. The most active preparation of AChE, which hydrolysed 13,500 μMmoles of acetylthiocholine/mg of protein/h, had an estimated molecular weight of 291,000 and was contaminated by a single protein component, as judged by disc gel electrophoresis.