期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1973
卷号：70
期号：12
页码：3749-3753
DOI：10.1073/pnas.70.12.3749
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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 {micro}mole/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.
关键词：( p -( m -bromophenyl)vinyl pyridinium ; mercurial-Sepharose columns
