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Isolement par chromatographie d'affinite de fractions membranaires specialisees, a partir de microsomes d'hepatocytes de chat
Author(s) -
Azzar G.,
Got R.
Publication year - 1978
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(78)81084-9
Subject(s) - chemistry , glucokinase , microsome , biochemistry , enzyme , adenylate kinase , golgi membrane , transferase , sepharose , vesicle , membrane
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 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.