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A novel adenosine triphosphatase isolated from RNA polymerase preparations of Escherichia coli. II. Enzymatic properties and molecular structure.

A novel adenosine triphosphatase isolated from RNA polymerase preparations of Escherichia coli. II. Enzymatic properties and molecular structure. Research Abstract Details 

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  • A novel adenosine triphosphatase isolated from RNA polymerase preparations of Escherichia coli. II. Enzymatic properties and molecular structure. Abstract Text:

    a ishihamaA Ishihama,t ikeuchiT Ikeuchi,a matsumotoA Matsumoto,s yamamotoS Yamamoto,

    An adenosinetriphosphatase (ATPase) [EC 3.6.1.3] copurified with the DNA-dependent RNA polymerase [EC 2.7.7.6] from Escherichia coli was isolated to apparent homogeneity and some of its functional as well as structural properties were examined. Although the novel ATPase exhibited metal requirements similar to those of Mg2+, Ca2+-ATPase, its response to NaN3 and antisera appeared completely different from that of the Mg2+, Ca2+-ATPase. The purified ATPase was found to be a large protein with a molecular weight of 9.3X10(5) daltons, composed of identical subunits of 7X10(4) daltons. When viewed under an electron microscope, the ATPase appeared to be very similar to material previously misidentified as the RNA polymerase. The physiological role of the novel ATPase, however, remains unclear.

    A novel adenosine triphosphatase isolated from RNA polymerase preparations of Escherichia coli. II. Enzymatic properties and molecular structure. Publishing Authors By Initials

    a ishihamaA Ishihama,t ikeuchiT Ikeuchi,a matsumotoA Matsumoto,s yamamotoS Yamamoto,

    For similar inorganic chemicals: elements: metals, alkali: sodium research abstracts see: inorganic chemicals: elements: metals, alkali: sodium research

    PUBMED ID PMID:

    MEDLINE DATE:

    A novel adenosine triphosphatase isolated from RNA polymerase preparations of Escherichia coli. II. Enzymatic properties and molecular structure. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: Journal of biochemistry

    VOLUME: 79

    Page Numbers: 927-37

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: May

    YEAR: 1976

    A novel adenosine triphosphatase isolated from RNA polymerase preparations of Escherichia coli. II. Enzymatic properties and molecular structure. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    A novel adenosine triphosphatase isolated from RNA polymerase preparations of Escherichia coli. II. Enzymatic properties and molecular structure. Keywords Mesh Terms:

    KEYWORDS: Sodium

    MESH TERMS: pharmacology

    Chemical & Substance for Abstract: A novel adenosine triphosphatase isolated from RNA polymerase preparations of Escherichia coli. II. Enzymatic properties and molecular structure. Information

    Substance Name: Adenosine Triphosphatases

    Registry Number: EC 3.6.1.-

    Grant and Affiliation Information for A novel adenosine triphosphatase isolated from RNA polymerase preparations of Escherichia coli. II. Enzymatic properties and molecular structure.

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    Country: JAPAN

    JAPAN Research PublicationJAPAN Research Publication

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    MEDLINETA: J Biochem

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