Author(s): Samir M. Khoja
Article publication date: 1987-08-01
Vol. 5 No. 2 (yearly), pp. 205-214.
100
Keywords
isoenzymes, phosphofructokinase, rats, mouse, intestine
Abstract
The regulatory properties of mouse jejunal mucosa phosphofructokinase have been studied in crude extracts freed from low molecular weight effectors on Sephadex G-100, and compared to those of the rat. Both isoenzymes displayed cooperativity with respect to fructose 6-phosphate at pH 7.0 in the presence of inhibitory concentrations of ATP. The rat isoenzyme was activated to a greater extent by AMP and P1 and inhibited to a greater extent by creatine phosphate than the mouse isoenzyme. Bothe isoenzymes were strongly activated by glucose 1,6-bisphosphate and strongly inhibited by citrate. The general similarity in properties of the two isoenzymes reflects the fact that both rat and mouse intestinal mucosa are characterised by high rates of aerobic glycolysis.