Phosphofructokinase activity and the binding of enzymes to glycogen particles in the perfused psoas muscle of the rabbit.
The activity of phosphofructokinase in the perfused rabbit psoas muscle was investigated after perfusion in the presence of either propranolol or isoproterenol, and after 48 hr starvation. The phosphofructokinase activities were correlated with the concentrations of glucose 1,6-bisphosphate in the muscles. A considerable fraction of enzymes of the glycogen metabolism and of phosphofructokinase was bound to glycogen particles. The extent of binding was not regulated by the glycogen content.
D000818:Animals; D005947:Glucose / Q000378:metabolism; D019298:Glucose-6-Phosphate / Q000031:analogs & derivatives*; D005958:Glucosephosphates / Q000378:metabolism; D006003:Glycogen / Q000378:metabolism*; D066298:In Vitro Techniques; D007700:Kinetics; D009132:Muscles / Q000201:enzymology* / Q000378:metabolism; D010477:Perfusion; D010732:Phosphofructokinase-1 / Q000378:metabolism*; D011485:Protein Binding; D011494:Protein Kinases / Q000378:metabolism; D011817:Rabbits
D005958:Glucosephosphates; D019298:Glucose-6-Phosphate; D006003:Glycogen; C016473:glucose-1,6-bisphosphate; D011494:Protein Kinases; D010732:Phosphofructokinase-1; D005947:Glucose