Reconstitution of adenosine triphosphatase of thermophilic bacterium from purified individual subunits.
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Summary
The ATPase activity reconstituted from alpha + beta + delta was thermolabile and insensitive to NaN3, whereas the activities obtained from mixtures containing beta and gamma were thermostable and sensitive to NaNs3, like the native ATPase.
- Type
- article
- Published
- 1977-05-25
- Cited by
- 145
- References
- 0
- Access
- Open access
- OpenAlex
- https://openalex.org/W1575474722
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:40518183
Keywords
Thermolabile, ATPase, BETA (programming language), Chemistry, Protein subunit
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Cited by
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- On the rotational brownian motion of a bacterial idle motor. II. Theory of fluorescence correlation spectroscopy.
- Assembled F1-(alpha beta ) and Hybrid F1-alpha 3beta 3gamma -ATPases from Rhodospirillum rubrum alpha, wild type or mutant beta, and chloroplast gamma subunits. Demonstration of Mg2+versus Ca2+-induced differences in catalytic site structure and function.
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- Physiology of thermophilic bacteria.
- Energy-transducing proteins in thermophilic biomembranes
- Protein Thermostability: Mechanism and Control Through Protein Engineering
- Mechanisms of thermophily.
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