Reconstitution of adenosine triphosphatase of thermophilic bacterium from purified individual subunits.

This publication has 28 references indexed in Scilit:

• Role of Mg2+ ions in the subunit structure and membrane binding properties of bacterial energy transducing ATPase
  Biochemical and Biophysical Research Communications, 1976
• ATPase of Escherichia coli: purification, dissociation, and reconstitution of the active complex from the isolated subunits
  Biochemistry, 1976
• Differentiation between mutants of Escherichia coli K12 defective in oxidative phosphorylation
  Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1975
• Restoration of coupling factor activity to Escherichia coli ATPase missing the delta subunit
  Biochemical and Biophysical Research Communications, 1975
• The structure of mitochondrial ATPase
  Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1973
• Light-stimulated incorporation of N-ethylmaleimide into coupling factor 1 in spinach chloroplasts
  Biochemistry, 1973
• Methods for purification of each subunit of the mitochondrial oligomycin-insensitive adenosine triphosphatase. IV
  Biochemistry, 1972
• Subunit structure and properties of two forms of adenosine triphosphatase released from Micrococcus,lysodeikticus membranes
  Biochemical and Biophysical Research Communications, 1972
• Membrane Adenosine Triphosphatase of Micrococcus lysodeikticus
  European Journal of Biochemistry, 1969
• A coupling factor in photophosphorylation
  Biochimica et Biophysica Acta, 1963