文章基本信息

标题：Purification and Properties of Mg2+-Ca2+ Adenosinetriphosphatase from Escherichia coli
本地全文：下载
作者：Nathan Nelson ; Baruch I. Kanner ; David L. Gutnick 等
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：1974
卷号：71
期号：7
页码：2720-2724
DOI：10.1073/pnas.71.7.2720
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：A procedure for the purification of Mg2+-Ca2+ adenosinetriphosphatase (EC 3.6.1.3 ) from E. coli, yielding relatively large amounts of highly active enzyme, is described. The enzyme consists of four nonidentical subunits. Trypsin treatment of purified enzyme yields a preparation consisting exclusively of the two larger subunits, which are sufficient for ATPase activity. Purified enzyme is inhibited by 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole; this inhibition is reversed by dithiothreitol, and the diazole is found preferentially associated with the {beta}-subunit of the enzyme. Antibody prepared against the trypsin-treated enzyme inhibited various ATP-dependent reactions as well as membrane-bound ATPase itself.
关键词：sulfhydryl reagent ; catalytic subunits ; antibody