A highly stable adenosine triphosphatase from a thermophillie bacterium. Purification, properties, and reconstitution.
Open Access
- 1 October 1975
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 250 (19), 7910-7916
- https://doi.org/10.1016/s0021-9258(19)40902-2
Abstract
No abstract availableKeywords
This publication has 34 references indexed in Scilit:
- Mitochondrial adenosine triphosphatase. Location of sulfhydryl groups and disulfide bonds in the soluble enzyme from beef heartBiochemistry, 1975
- Mitochondrial adenosine triphosphataseJournal of Bioenergetics and Biomembranes, 1975
- The structure of mitochondrial ATPaseBiochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1973
- Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersionBiochemistry, 1972
- Reconstitution of oxidate phophorylationBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1972
- Allosteric nature of thermostable phosphofructokinase from an extreme thermophilic bacteriumBiochemistry, 1972
- Studies on an ATPase of thermophilic bacteria: I. Purification and propertiesBiochimica et Biophysica Acta (BBA) - Enzymology, 1970
- DISC ELECTROPHORESIS‐I BACKGROUND AND THEORY*Annals of the New York Academy of Sciences, 1964
- A correlation between amino acid composition and protein structureJournal of Molecular Biology, 1964
- Thermal enzymes. IV. Partial separation of an adenosinetriphosphatase from an apyrase fractionArchives of Biochemistry and Biophysics, 1952