A membrane-bound ATPase from Halobacterium halobium: purification and characterization.

A membrane-bound ATPase from Halobacterium halobium: purification and characterization. Research Abstract Details 

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A membrane-bound ATPase from Halobacterium halobium: purification and characterization. Abstract Text:

T Nanba,Y Mukohata,

An ATPase was newly identified on the inner face of the plasma membrane of the extremely halophilic archaebacterium Halobacterium halobium. The enzyme was released into an alkaline EDTA solution and purified by several chromatographic steps in the presence of sulfate at 1 M or over. The molecular weight of the native enzyme was around 320,000; it is most likely composed of two pairs (alpha 2 beta 2) of 86,000 (alpha) and 64,000 (beta) subunits. The enzyme hydrolyzed ATP and other nucleoside triphosphates but neither ADP nor AMP. The enzyme required divalent cations, among which Mn2+ was most effective (Mg2+ activated 35% of Mn2+). The ATPase activity was optimum at pH between 5.5 and 6, particularly in a nearly saturated Na2SO4 (or Na2SO3) solution, while it was very low in a chloride salt solution even at 4 M at any pH. The Km value for ATP was 1.4 mM and the K1 value for ADP (competitive to ATP) was 0.08 mM. Neither azide (a specific inhibitor for F0F1-and F1-ATPase) nor vanadate (for E1E2-ATPase) inhibited the enzyme. The ATPase was stable at high concentrations of sulfate. At low concentrations of salts, or at low temperatures even in high NaCl concentrations, the enzyme was inactivated. Although the ATPase isolated here from halobacterial membrane has such unusual characteristics, it is the most probable candidate for the (catalytic part of) halobacterial ATP synthase, which differs from F0F1-ATPase/synthase (Mukohata et al. (1986) J. Biochem. 99, 1-8; Mukohata and Yoshida (1987) J. Biochem. 101, 311-318).

A membrane-bound ATPase from Halobacterium halobium: purification and characterization. Publishing Authors By Initials

T Nanba,Y Mukohata,

For similar natural sciences: chemistry: chemistry, physical: molecular weight research abstracts see: natural sciences: chemistry: chemistry, physical: molecular weight research

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A membrane-bound ATPase from Halobacterium halobium: purification and characterization. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 102

Page Numbers: 591-8

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Sep

YEAR: 1987

A membrane-bound ATPase from Halobacterium halobium: purification and characterization. Information

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LANGUAGE: eng

NlmUniqueID: 376600

A membrane-bound ATPase from Halobacterium halobium: purification and characterization. Keywords Mesh Terms:

KEYWORDS: Molecular Weight

MESH TERMS: enzymology

Chemical & Substance for Abstract: A membrane-bound ATPase from Halobacterium halobium: purification and characterization. Information

Substance Name: Adenosine Triphosphatases

Registry Number: EC 3.6.1.-

Grant and Affiliation Information for A membrane-bound ATPase from Halobacterium halobium: purification and characterization.

AFFILIATION: Department of Biology, Faculty of Science, Osaka University.

Country: JAPAN

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MEDLINETA: J Biochem

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