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J. Biol. Chem., Vol. 255, Issue 22, 10576-10578, Nov, 1980
GD Reinhart
The influence of polyethylene glycols on the kinetics of purified rat liver
phosphofructokinase was examined because polyethylene glycol often has an
associative influence on proteins without specifically interacting with
them. Polyethylene glycol was found to prevent or slow the spontaneous
inactivation, due to subunit dissociation, of rat liver phosphofructokinase
which occurs at low protein concentration (10 microgram/ml) in an isotonic,
pH 7 buffer in the absence of substrates. This protection is favored by
increasing size and concentration of polyethylene glycol. Inclusion of
polyethylene glycol in kinetic assays of rat liver phosphofructokinase had
little effect on maximal velocity determined under optimal conditions at pH
8. However, the Km value for fructose 6-phosphate measured at pH 7 and 3 mM
MgATP was dramatically lowered with increasing polyethylene glycol
concentration. The results support the proposal that more aggregated forms
of rat liver phosphofructokinase have a decreased Km value for fructose
6-phosphate when assayed with inhibiting concentrations of MgATP.
Influence of polyethylene glycols on the kinetics of rat liver phosphofructokinase
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