Binding of nucleotides to purified coupling factor-latent ATPase from Mycobacterium phlei.
Open Access
- 1 February 1977
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 252 (3) , 1084-1091
- https://doi.org/10.1016/s0021-9258(19)75209-0
Abstract
No abstract availableThis publication has 32 references indexed in Scilit:
- Characterization of nucleotide binding sites on chloroplast coupling factor 1Biochemistry, 1975
- Adenosine triphosphatase from rat liver mitochondria: Separate sites involved in ATP hydrolysis and in the reversible, high affinity binding of ADPBiochemical and Biophysical Research Communications, 1975
- Purification and properties of membrane-bound coupling factor-latent ATPase from mycobacterium phleiJournal of Supramolecular Structure, 1975
- Tight binding of adenine nucleotides to beef-heart mitochondrial ATPaseBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1973
- Equilibrium binding of nucleotides to beef heart mitochondrial adenosine triphosphataseBiochemistry, 1973
- Molecular weight, amino acid composition and other properties of membrane-bound ATPase fromBacillus megaterium KMBiochimica et Biophysica Acta (BBA) - Biomembranes, 1973
- Purification of a factor for both aerobic‐driven and ATP‐driven energy‐dependent transhydrogenases of Escherichia coliFEBS Letters, 1972
- Subunit structure and properties of two forms of adenosine triphosphatase released from Micrococcus,lysodeikticus membranesBiochemical and Biophysical Research Communications, 1972
- Reassessment of the molecular weight of mitochondrial ATPase from beef heartFEBS Letters, 1971
- THE ATTRACTIONS OF PROTEINS FOR SMALL MOLECULES AND IONSAnnals of the New York Academy of Sciences, 1949