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- W378600018 abstract "Glyeolaldehyde dehydrogenase, an enzyme involved in vitamin B6 biosynthesis, was partially purified from the wild type strain of Escherichia coli B. The enzyme was separated into three fractions (glyeolaldehyde dehydrogenases A, B and C) by DEAE-cellulose column chromatography. The enzymes B and C, which were eluted by 0.1 m potassium phosphate buffer plus 0.1 m NaCl and by that plus 0.2 m NaCl, respectively, lacked in the cell-free extract of a pyridoxine auxotrophic strain, E. coli B WG3, The enzyme A, which was eluted by 0.1 m potassium phosphate buffer has a broad specificity for substrate. On the other hand, the enzyme B or C is relatively specific to glyeolaldehyde. The enzymes A, B and C could be defined as isozymes with enzymatic characterization." @default.
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- W378600018 date "1978-01-01" @default.
- W378600018 modified "2023-09-28" @default.
- W378600018 title "Studies on vitamin B6 metabolism in microorganisms. XIII. Separation and characterization of glycolaldehyde dehydrogenase isozymes in Escherichia coli B." @default.
- W378600018 doi "https://doi.org/10.1271/bbb1961.42.63" @default.
- W378600018 hasPublicationYear "1978" @default.
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