Conversion of stable atpase to labile atpase by acetylation, and the αβ and αγ subunit complexes during its reconstitution
Authors:
- Yasuo KagawaYKYasuo Kagawa
- Noriko NukiwaNNNoriko Nukiwa
- 1 June 1981
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 100 (3) , 1370-1376
Abstract
No abstract availableThis publication has 18 references indexed in Scilit:
- pH dependence of stability of the wild-type tryptophan synthase α-subunit and two mutant proteins (Glu49 → Met or Gln)Journal of Molecular Biology, 1980
- Functional arginine residues and carboxyl groups in the adenosine triphosphatase of the thermophilic bacterium PS-3Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1980
- Reconstitution of ATPase from the isolated subunits of coupling factor F1's of Escherichia coli and thermophilic bacterium PS3Biochemical and Biophysical Research Communications, 1980
- Intersubunit interactions in proton-translocating adenosine triphosphatase as revealed by hydrogen-exchange kineticsBiochemistry, 1980
- [84] Soluble ATPase (F1) from a thermophilic bacterium: Purification, dissociation into subunits, and reconstitution from individual subunits1979
- Another look at the cold lability of enzymesTrends in Biochemical Sciences, 1978
- Oxidative Phosphorylation and PhotophosphorylationAnnual Review of Biochemistry, 1977
- ATPase of Escherichia coli: purification, dissociation, and reconstitution of the active complex from the isolated subunitsBiochemistry, 1976
- Dissociation and Reassembly of the Inner Mitochondrial Membrane1974
- [83] Preparation of 3H-Acetyl-ATPase (coupling factor 1)1967