Purification and Some Properties of Sucrose Phosphorylase from Leuconostoc mesenteroides(Biological Chemistry)
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概要
- 論文の詳細を見る
Sucrose phosphorylase (EC 2.4.1.7) was purified to homogeneity from Leuconostoc mesenteroides cells with a specific activity of 173.8 units per mg protein by ammonium sulfate fractionation, anion exchange HPLC on TSKgel DEAE-5PW, and hydrophobic HPLC on TSKgel Ether-5PW. The purified enzyme was an acidic protein having an isoelectric point of pH 4.6 and s^0_<20,W> of 4.34S. The molecular weight of this enzyme was estimated to be 56,400 by sedimentation equilibrium, 55,000 by SDS-polyacrylamide gel electrophoresis, and HPLC gel filtration on TSKgel G3000SW, suggesting that the enzyme is a monomeric protein. With regard to molecular weight, amino acid composition, and N-terminal amino acid sequence of 30 residues, this enzyme is close to the glucosyltransferase A of Streptococcus mutans.
- 社団法人日本農芸化学会の論文
- 1991-07-23
著者
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NAKAMURA Kazuo
Research Institute for Applied Mechanics, Kyushu University
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KIKUCHI Mamoru
Research and Development Division, Kikkoman Corporation
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Koga Takuro
Research And Development Division Kikkoman Corporation
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Kikuchi Mamoru
Research & Development Division Kikkoman Corporation
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Kitao Satoshi
Research And Development Division Kikkoman Corporation
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SHIROKANE Yoshio
Research and Development Division, Kikkoman Corporation
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MIZUSAWA Kiyoshi
Research and Development Division, Kikkoman Corporation
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Mizusawa Kiyoshi
Research And Development Division Kikkoman Corporation
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Mizusawa Kiyoshi
Research & Development Division Of Kikkoman Corpration
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Shirokane Yoshio
Research And Development Division Kikkoman Corporation
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Shirokane Yoshio
Research & Development Division Kikkoman Corporation
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Nakamura Kazuo
Research And Development Division Kikkoman Corporation
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Nakamura Kazuo
Research & Development Division Kikkoman Corporation
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