Purification and Characterization of Mannose Isomerase from Agrobacterium radiobacter M-1
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概要
- 論文の詳細を見る
A mannose isomerase from Agrobacterium radiobacter M-1 (formerly Pseudomonas sp. MI) was purified to electrophoretic homogeneity and characterized. A cell-free extract was separated by ammonium sulfate fractionation, Butyl-Toyopearl 650M, DEAE-Sepharose and hydroxylapatite column chromatography. Its molecular mass was estimated to be 44 kDa by SDS-PAGE and 90 KDa by gel filtration, in which the enzyme is most likely a dimer composed of two identical subunits. The purified enzyme had an optimum pH at 8.0,an optimum temperature at 60℃, a pI of 5.2 and a K_m of 20 mM, and specifically converted D-mannose and D-lyxose to ketose. The N-terminal amino acid sequence was identified.
- 社団法人日本農芸化学会の論文
- 2001-03-23
著者
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MAEDA Kazuhiko
Department of Chemical System Engineering, School of Engineering, The University of Tokyo
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HIROSE Jun
Department of Immunology, Pharmacology Research Labs, Astellas Pharma, Inc.
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Takasaki Yoshiyuki
Department of Materials Science, Faculty of Engineering, Miyazaki University
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YOKOI HARUHIKO
Department of Materials Science, Faculty of Engineering, Miyazaki University
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Takasaki Yoshiyuki
Department Of Applied Chemistry Faculty Of Engineering Miyazaki University
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Takasaki Yoshiyuki
Laboratory Of Biophysical Chemistry College Of Agriculture Osaka Prefecture University:dainippon Phe
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Hirose Jun
Department Of Applied Chemistry Miyazaki University
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Maeda K
Department Of Applied Chemistry Faculty Of Engineering Miyazaki University
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Yokoi Haruhiko
Department Of Applied Chemistry Miyazaki University
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Yokoi Haruhiko
Department Of Applied Chemistry Faculty Of Engineering University Of Miyazaki
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Hirose Jun
Department Of Agricultural Chemistry Faculty Of Agriculture Tamagawa University
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Maeda Kazuhiko
Department Of Applied Chemistry Faculty Of Engineering Miyazaki University
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