Purification and properties of Mg2+ Ca2+ adenosinetriphosphatase from Escherichia coli

N. Nelson, B. I. Kanner, D. L. Gutnick

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A procedure for the purification of Mg2 Ca2 adenosinetriphosphatase (EC from E. coli, yielding relatively large amounts of highly active enzyme, is described. The enzyme consists of 4 non identical subunits. Trypsin treatment of purified enzyme yields a preparation consisting exclusively of the 2 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 β subunit of the enzyme. Antibody prepared against the trypsin treated enzyme inhibited various ATP dependent reactions as well as membrane bound ATPase itself.

Original languageEnglish
Pages (from-to)2720-2724
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number7
StatePublished - 1974
Externally publishedYes


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