Glycogen phosphorylase has been purified from rabbit liver by a simplified procedure which
depends on the initial separation of the enzyme from a crude extract by centrifuging it as a
complex with particulate glycogen. Initial rates have been measured with varied
concentrations of both substrates in each reaction direction. The data were analyzed with
double reciprocal plots and secondary plots of intercepts and slopes to yield the eight
Dalziel kinetic coefficients. Inhibition by uridine diphosphoglucose is competitive with …