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

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

doi:10.1073/pnas.71.7.2720

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

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

Research output: Contribution to journal › Article › peer-review

79 Scopus citations

Abstract

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 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 language	English
Pages (from-to)	2720-2724
Number of pages	5
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	71
Issue number	7
DOIs	https://doi.org/10.1073/pnas.71.7.2720
State	Published - 1974
Externally published	Yes

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10.1073/pnas.71.7.2720

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abstract = "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 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.",

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AU - Kanner, B. I.

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N2 - 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 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.

AB - 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 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.

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

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