Extraction and purification of the beta subunit and an active alpha beta-core complex from the spinach chloroplast CFoF1-ATP synthase.

This publication has 36 references indexed in Scilit:

• The α1β1 heterodimer of ATP synthase
  Biochemical and Biophysical Research Communications, 1990
• α₃β₃ complex of thermophilic ATP synthase Catalysis without the γ‐subunit
  FEBS Letters, 1989
• Biochemical and proton NMR characterization of the isolated functional beta-subunit of coupling factor one from spinach chloroplasts
  Biochemical and Biophysical Research Communications, 1987
• Sequential removal and reconstitution of subunits β and γ from a membrane-bound Fo·Fl-ATP synthase
  Biochemical and Biophysical Research Communications, 1981
• Cold Storage of Isolated Class C Chloroplasts
  Plant Physiology, 1979
• Reconstitution of ATPase activity from the isolated α, β, and γ subunits of the coupling factor, F1, of Escherichia coli
  Biochemical and Biophysical Research Communications, 1977
• A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
  Analytical Biochemistry, 1976
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
  Nature, 1970
• Simple Microassay of Protein with Membrane Filter
  Nature, 1967
• Photophosphorylation by swiss-chard chloroplasts
  Biochimica et Biophysica Acta, 1959