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 |
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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 > School of Molecular Biosciences |
Journal Name: | Biochemical Journal |
Publisher: | Portland Press |
ISSN: | 0264-6021 |
ISSN (Online): | 1470-8728 |
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