Adenosine 5'-phosphosulfate kinase from Penicillium chrysogenum. Determining ligand dissociation constants of binary and ternary complexes from the kinetics of enzyme inactivation.

This publication has 18 references indexed in Scilit:

• Determination of dissociation constants for enzyme-reactant complexes for NAD-malic enzyme by modulation of the thiol inactivation rate
  Biochemistry, 1984
• The inhibition of acetylcholinesterase by arsenite and fluoride
  Archives of Biochemistry and Biophysics, 1983
• ATP sulfurylase from Penicillium chrysogenum: Measurements of the true specific activity of an enzyme subject to potent product
  Archives of Biochemistry and Biophysics, 1983
• Determination of the rate constant of enzyme modification by measuring the substrate reaction in the presence of the modifier
  Biochemistry, 1982
• A kinetic investigation of the aps-kinase from Chlamydomonas reinhardii CW 15
  Phytochemistry, 1981
• Enzymatic sulfation of steroids
  Analytical Biochemistry, 1979
• Affinity Labelling of Rat‐Muscle Hexokinase Type II by a Glucose‐Derived Alkylating Agent
  European Journal of Biochemistry, 1979
• APPENDIX
  European Journal of Biochemistry, 1979
• The acceleration of methanesulfonylation of acetylcholinesterase with cationic accelerators as an electrostatic effect
  Biochimica et Biophysica Acta (BBA) - Enzymology, 1978
• A new, rapid, and sensitive assay for adenosine 5′-phosphosulphate (APS) kinase
  Analytical Biochemistry, 1975