[Liberation and reassociation of the microsomal membrane glucokinase in cat liver].
Biochimie, 1977;59(3):303-9.
PMID: 196677
Impact factor: 4.372
Abstract
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.
MeSH terms
Animals; Binding Sites; Cats; Diphosphates; Glucokinase; Isoelectric Focusing; Kinetics; Membranes; Microsomes, Liver; Polyethylene Glycols; Protein Binding; Ribonucleotides; Solubility
More resources
EndNote: Download