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Purification and Characterization of Glucokinase in Escherichia coli B
Authors:Yasuki Fukuda  Shotaro Yamaguchi  Makoto Shimosaka  Kousaku Murata  Akira Kimura
Institution:Research Institute for Food Science, Kyoto University, Uji, Kyoto 611, Japan
Abstract:Glucokinase was purified from Escherichia coli B cells dosed with a hybrid plasmid carrying the gene for glucokinase. The enzyme was purified about 170-fold and was homogeneous on polyacrylamide gel electrophoresis. The enzyme was 49,000 in molecular weight and consisted of two subunits having a molecular weight of 24,500. The glucokinase catalyzed phosphorylation of D-glucose, D-mannose, D-glucosamine, and 2-deoxy-D-glucose, consuming ATP as a phosphoryl donor. Besides ATP, other nucleoside triphosphates such as ITP, GTP and UTP were also utilized as phosphoryl donors. The enzyme required free sulfhydryl groups and Mg2+ for activity. Other properties of the glucokinase were characterized and compared with those of glucokinases from various sources.
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