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

TY - JOUR

T1 - Effects of phosphorylation on the kinetic properties of rat liver fructose-1,6-bisphosphatase

AU - Meek, D. W.

AU - Nimmo, H. G.

PY - 1984/8/15

Y1 - 1984/8/15

N2 - 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.

AB - 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.

M3 - Article

C2 - 6089751

SN - 0264-6021

VL - 222

SP - 125

EP - 130

JO - Biochemical Journal

JF - Biochemical Journal

IS - 1

ER -