[Liberation and reassociation of the microsomal membrane glucokinase in cat liver].
The particulate glucokinase of cat liver is shown to be microsomal. The activity is readily solubilized by glucose-6-phosphate, ATP, pyrophosphate, high salt concentrations and, to a lesser extent, ribonucleoside triphosphates. The solubilization by glucose-6-phosphate is inhibited by Pi. Solubilizations by ATP and glucose-6-phosphate differ in their sensitivity to temperature changes; they are relatively specific for glucokinase as compared to solubilization by detergent (Triton X 100). The enzyme can be bound again to previously eluted microsomal membranes. Treatment of membrane with trypsin, at 0 degrees C, destroys the ability to rebind the enzyme to the membrane. It is suggested that electrostatic forces are of considerable importance for the binding of glucokinase to a possible protein binding site in the membrane.
D000818:Animals; D001665:Binding Sites; D002415:Cats; D011756:Diphosphates; D005941:Glucokinase / Q000302:isolation & purification / Q000378:metabolism; D007525:Isoelectric Focusing; D007700:Kinetics; D008566:Membranes / Q000201:enzymology; D008862:Microsomes, Liver / Q000201:enzymology*; D011092:Polyethylene Glycols; D011485:Protein Binding; D012265:Ribonucleotides; D012995:Solubility
D011756:Diphosphates; D012265:Ribonucleotides; D011092:Polyethylene Glycols; D005941:Glucokinase
Libération et réassociation à la membrane de la glucokinase microsomique du foie de chat.