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. 1973 Dec;70(12 Pt 1-2):3749–3753. doi: 10.1073/pnas.70.12.3749

The Purification of Choline Acetyltransferase of Squid-Head Ganglia

S S Husain 1, Henry G Mautner 1
PMCID: PMC427320  PMID: 4521199

Abstract

Choline acetyltransferase (EC 2.3.1.6) isolated from the head ganglia of squid could be purified by use of mercurial-Sepharose columns as well as Sepharose columns to which the enzyme inhibitor p-(m-bromophenyl)vinyl pyridinium had been attached. These columns, in conjunction with 30-55% ammonium sulfate precipitation, 40-30% ammonium sulfate extraction, chromatography on sulfopropyl-Sephadex and on cellulose phosphate and hydroxylapatite columns, led to the isolation of three factions of choline acetyltransferase ranging in activity from 1000 to 4000 μmole/mg of protein/per hr. Polyacrylamide gel electrophoresis suggests that two of these fractions are homogeneous. The squid choline acetyltransferase is different from the mammalian-brain enzymes in having a larger molecular weight under the conditions used and in being relatively poorly inhibited by styryl pyridinium compounds.

Keywords: (p-(m-bromophenyl)vinyl pyridinium, mercurial-Sepharose columns

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Selected References

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