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

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.

SUBMITTER: Meek DW 

PROVIDER: S-EPMC1144152 | biostudies-other | 1984 Aug

REPOSITORIES: biostudies-other