Abstract
The association-dissociation equilibrium of glycogen phosphorylase b in the presence of AMP and inorganic phosphate was studied at 25°C. The effect of P i , AMP and enzyme concentrations on the kinetic and equilibrium constants have been investigated. The dimerization kinetic constant did not depend either on substrate or allosteric activator concentrations, whereas the equilibrium and tetramerization kinetic constants were strongly dependent on both AMP and P i concentrations. Experimental results shown in this paper also support the proposition that formation of tetrameric phosphorylase b is directly related to the formation of dimeric phosphorylase b in its E 2 conformation ( R), which is the catalytically active conformation.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: International Journal of Biological Macromolecules
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
