title: [Isolation by affinity chromatography of specialized membrane fractions from cat liver microsomes].
abstract: Microsomal glucokinase is solubilized by incubation in the presence of several metabolites. After solubilization of the enzymes, the membranes present free sites for specific binding of glucokinase, therefore, they can be purified by affinity chromatography on Sepharose--ATP-glucokinase. This method yields membranous vesicles which contain, in addition to glucokinase, uridylyl-transferase, phosphoglucomutase, sialyl-transferase and adenylate cyclase. Galactosyl-transferase, glucose-6-phosphatase and NADPH cytochrome c reductase are absent. It appears that functionally related enzyme from UDP-glucose biosynthesis are aggregated onto specific patches of the membrane, most likely from Golgi apparatus.
mesh_terms: D000818:Animals; D001665:Binding Sites; D002415:Cats; D002846:Chromatography, Affinity / Q000379:methods; D011756:Diphosphates / Q000378:metabolism; D005941:Glucokinase / Q000378:metabolism*; D006056:Golgi Apparatus / Q000201:enzymology; D007425:Intracellular Membranes / Q000201:enzymology; D008862:Microsomes, Liver / Q000032:analysis* / Q000201:enzymology; D014532:Uridine Diphosphate Glucose / Q000378:metabolism
chemical_list: D011756:Diphosphates; D005941:Glucokinase; D014532:Uridine Diphosphate Glucose
vernacular_title: Isolement par chromatographie d'affinité de fractions membranaires specialisées, à partir de microsomes d'hepatocytes de chat.