The use of the ultracentrifuge to determine the catalytically competent forms of enzymes with more than one oligomeric structure. Multiple reacting forms of pyruvate carboxylase from chicken and rat liver.

This publication has 26 references indexed in Scilit:

• Pyruvate Carboxylase: Effect of Reaction Components and Analogues of Acetyl‐Coenzyme A on the Rate of Inactivation in the Presence and Absence of Trinitrobenzene Sulphonate
  European Journal of Biochemistry, 1977
• Determination of Molecular Weight and Molecular Structurof Rat-Liver Pyruvate Carboxylase
  European Journal of Biochemistry, 1976
• The use of sedimentation coefficients to distinguish between models for protein oligomers
  Biophysical Chemistry, 1976
• Isolation and characterization of pyruvate carboxylase from Azotobacter vinelandii OP
  Archives of Biochemistry and Biophysics, 1974
• Desensitization of pyruvate carboxylase against acetyl CoA stimulation by chemical modification
  Biochemical and Biophysical Research Communications, 1973
• Pyruvate carboxylase from rat liver: Catalytic properties in the absence, and at low concentrations, of acetyl-CoA
  Biochemical and Biophysical Research Communications, 1972
• Pyruvate carboxylase from chicken liver: Effects of sulfate and other anions on catalytic activity and structural parameters
  Archives of Biochemistry and Biophysics, 1972
• Analytical‐Band Centrifugation of an Active Enzyme‐Substrate Complex
  European Journal of Biochemistry, 1971
• Pyruvate carboxylase. XIII. Reversible inactivation by cold
  Biochemistry, 1969
• Theory and practice of the analytical centrifugation of an active substrate–enzyme complex
  Biopolymers, 1967