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.
| Original language | English |
|---|---|
| Pages (from-to) | 125-130 |
| Number of pages | 6 |
| Journal | Biochemical Journal |
| Volume | 222 |
| Issue number | 1 |
| Publication status | Published - 15 Aug 1984 |