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PMID: 6089751 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

The Biochemical journal ·Vol. 222 ·No. 1 ·1984-08-15 ·Pages 125-30

Meek DW, Nimmo HG

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.

MeSH Terms
Animals Chromatography, Affinity Fructose-Bisphosphatase/isolation & purification,metabolism Fructosediphosphates/metabolism Kinetics Liver/enzymology Phosphorylation Rats Rats, Inbred Strains Triazines
Chemicals
Fructosediphosphates Triazines procion red HE-3B Fructose-Bisphosphatase fructose-1,6-diphosphate
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Meek D W
Nimmo H G
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27 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2220125
Published
1984-08-15
Pages
125-30
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1144152
Subset
IM
External Links
PubMed source DOI: 10.1042/bj2220125 PMC Full Text View journal details
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