Inactivation of glycogen phosphorylase of human polymorphonuclear leukocytes.

Glycogen phosphorylase of human polymorphonuclear leukocytes is dephosphorylated during incubation of a gel-filtered cell extract. The dephosphorylated enzyme (b form) retains 25 per cent of the activity of the phosphoenzyme (a form) when measured without AMP but a high glucose-1-phosphate concentrations. The ratio of activity -AMP/+AMP for the a enzyme is 0.8-1.0 and for the b enzyme 0.2. Leukocyte phosphorylase is not activated by -SH groups, but the b enzyme is stimulated by 0.4 mol/1 Na2SO4. The phosphatase which catalyzes the conversion of phosphorylase a to b is inhibited by glucose-1-phosphate and AMP both a 14 degrees C and 25 degrees C. Glucose counteracts the AMP inhibition but not the glucose-1-phosphate inhibition at both temperatures. Glucose alone had no effect at 25 degrees C, but it accelerated the phosphatase reaction at 14 degrees C. Glucose-6-phosphate or glycogen alone or in the presence of AMP or glucose-1-phosphate did not affect the phosphatase reaction. From previous and present experiments it is concluded that the phosphorylase of human polymorphonuclear leukocytes is closely related to liver phosphorylase and that the inactivation of the enzyme is mainly controlled by AMP and glucose.