The ammonium sulfate activation of phosphorylase b

D D Leonidas; N G Oikonomakos; A C Papageorgiou; A Xenakis; C T Cazianis; F Bem

doi:10.1016/0014-5793(90)80627-u

The ammonium sulfate activation of phosphorylase b

FEBS Lett. 1990 Feb 12;261(1):23-7. doi: 10.1016/0014-5793(90)80627-u.

Authors

D D Leonidas¹, N G Oikonomakos, A C Papageorgiou, A Xenakis, C T Cazianis, F Bem

Affiliation

¹ Biological Research Center, National Hellenic Research Foundation, Athens, Greece.

PMID: 2155134
DOI: 10.1016/0014-5793(90)80627-u

Abstract

The ammonium sulfate activation of phosphorylase b has been studied. Ammonium sulfate, when present in high concentrations, induces properties of phosphorylase a in phosphorylase b, such as an enhanced affinity for AMP, a reversal of the glucose-6-P inhibition and enzyme tetramerization. The data are consistent with the interpretation that sulfates bind to the Ser-14 site and the sulfate-protein interactions at this site are responsible for activation of phosphorylase b.

MeSH terms

Adenosine Monophosphate / pharmacology
Ammonium Sulfate / pharmacology*
Animals
Electron Spin Resonance Spectroscopy
Enzyme Activation / drug effects
Glucosephosphates / metabolism
Kinetics
Macromolecular Substances
Muscles / enzymology*
Phosphorylase b / metabolism*
Phosphorylases / metabolism*
Rabbits
Ultracentrifugation

Substances

Glucosephosphates
Macromolecular Substances
Adenosine Monophosphate
glucose-1-phosphate
Phosphorylase b
Phosphorylases
Ammonium Sulfate