Purification and Characterization of Glucokinase in Escherichia coli B
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概要
- 論文の詳細を見る
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.
- 社団法人 日本農芸化学会の論文
著者
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Murata Kousaku
Research Institute For Food Science Kyoto Univeristy
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Shimosaka Makoto
Research Institute For Food Science Kyoto University
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FUKUDA Yasuki
Research Institute for Food Science, Kyoto University
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Yamaguchi Shotaro
Research And Development Division Amano Pharmaceutical Co. Ltd.
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Kimura Akira
Research Center for Solar Energy Chemistry, Osaka University, 1-3 Machikaneyama, Toyonaka, Osaka 560-8531, Japan
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