Purification and Properties of NADPH-Linked L-Sorbose Reductase from Gluconobacter melanogenus N44-1(Biological Chemistry)
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概要
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NADPH-Linked L-sorbose reductase from the cytosol fraction of Gluconobacter melanogenus N44-1, which is a 2-keto-L-gulonic acid producer from L-sorbose or D-sorbitol, was purified about 500-fold by DEAE-Cellulose, Blue Sepharose, and DEAE-Sepharose column chromatographies. The purified enzyme was entirely homogeneous on polyacrylamide gel and SDS gel electrophoresis. NADPH and NADP were specifically required for the reduction and oxidation of the substrate, respectively. The apparent molecular weight was 60,000 by Sephadex G-200 column chromatography, and that of its subunit was 60,000 by SDS-gel electrophoresis. The pH optimum for the reduction of L-sorbose and D-fructose was 7.0. The pH optimum for the oxidation of D-sorbitol to L-sorbose and D-mannitol to D-fructose was 10.0-10.5.
- 1991-08-23
著者
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Fujiwara Akiko
Department of Molecular Biotechnology, Graduate School of Advanced Sciences of Matter, Hiroshima Uni
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Fujiwara A
Department Of Applied Microbiology Nippon Roche Research Center
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Hoshino Tatsuo
Departments of Medicine, Keio University and The Lankenau Hospital
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Fujiwara Akiko
Department Of Applied Microbiology Nippon Roche Research Center
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Hoshino T
Department Of Applied Microbiology Nippon Roche Research Center
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Sugisawa Teruhide
Department of Applied Microbiology, Nippon Roche Research Center
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Hoshino Tatsuo
Department Of Applied Microbiology Nippon Roche Research Center
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Fujiwara Masahiro
Department Of Applied Microbiology Nippon Roche Research Center
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Sugisawa T
Nippon Roche Res. Center Kanagawa Jpn
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Sugisawa Teruhide
Department Of Applied Microbiology Nippon Roche Research Center
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