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

Meek, D.W. and Nimmo, H.G. (1984) Effects of phosphorylation on the kinetic properties of rat liver fructose-1,6-bisphosphatase. Biochemical Journal, 222(1), pp. 125-130. (doi: 10.1042/bj2220125) (PMID:6089751) (PMCID:PMC1144152)

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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.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Nimmo, Professor Hugh
Authors: Meek, D.W., and Nimmo, H.G.
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
Journal Name:Biochemical Journal
Publisher:Portland Press
ISSN:0264-6021
ISSN (Online):1470-8728

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