Rate and equilibrium constants of the tetramerization process of phosphorylase b. Influence of AMP and Mg2+.
The association-dissociation equilibrium of phosphorylase b at different enzymatic concentrations has been studied at 25 degrees C in this paper, pointing out how this equilibrium is affected by both AMP and Mg2+ concentrations. It has also been proved that association of phosphorylase b in the presence of AMP and Mg2+ follows second-order and first-order rate laws in the direction of tetramerization and dimerization, respectively. Rate constants have also been calculated and their dependence upon protein, AMP and Mg2+ concentrations studied thoroughly.
D000249:Adenosine Monophosphate / Q000494:pharmacology*; D000818:Animals; D007700:Kinetics; D046911:Macromolecular Substances; D008274:Magnesium / Q000494:pharmacology*; D008433:Mathematics; D009132:Muscles / Q000201:enzymology*; D010763:Phosphorylase b / Q000378:metabolism*; D006005:Phosphorylases / Q000378:metabolism*; D011817:Rabbits
D046911:Macromolecular Substances; D000249:Adenosine Monophosphate; D010763:Phosphorylase b; D006005:Phosphorylases; D008274:Magnesium