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PARTIAL CHARACTERIZATION OF SOLUBLE ACETYLCHOLINESTERASE ISOENZYMES OF THE RAT BRAIN
Author(s) -
Bajgar J.,
ŽIžkovský V.
Publication year - 1971
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.1471-4159.1971.tb03734.x
Subject(s) - acetylthiocholine , acetylcholinesterase , isozyme , butyrylcholinesterase , chromatography , biochemistry , chemistry , enzyme , hydrolysis , electrophoresis , cholinesterase , extraction (chemistry) , agar gel , biology , microbiology and biotechnology , aché , pharmacology
(1) The 105,000 g supernatant fluid obtained from rat brain was separated by agar‐gel electrophoresis. (2) Three isoenzymes, capable of hydrolysing acetylthiocholine, one of them also hydrolysing butyrylthiocholine, were detected. (3) The pH optima and K m for hydrolysis of acetyl‐ and butyrylthiocholine by the supernatant fluid were determined. (4) After extraction of acetylcholinesterase isoenzymes from the gel, individual isoenzymes were characterized by pH optima and K m values. (5) Two of the enzymes were characterized as acetylcholinesterase (EC 3.1.1.7) and one as butyrylcholinesterase (EC 3.1.1.8).