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. 1984 Aug 15;222(1):125–130. doi: 10.1042/bj2220125

Effects of phosphorylation on the kinetic properties of rat liver fructose-1,6-bisphosphatase.

D W Meek, H G Nimmo
PMCID: PMC1144152  PMID: 6089751

Abstract

A new purification procedure for rat liver fructose-1,6-bisphosphatase that involves use of Procion Red-Sepharose is described. The purified enzyme was homogeneous, had a subunit Mr of 40 000-41 000 and seemed to be undegraded. The enzyme could be phosphorylated by cyclic AMP-dependent protein kinase with a stoicheiometry of one per subunit. Phosphorylation caused a 2-fold decrease in the Km of the enzyme for fructose 1,6-bisphosphate, but did not affect its allosteric responses to AMP, Mg2+ and fructose 2,6-bisphosphate.

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Selected References

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