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- W1996009886 abstract "UDP-Galactose 4′-epimerase was purified ca 800-fold through a multi-step procedure which included affinity chromatography using NAD+ -Agarose. Three forms of the enzyme were separated by gel-filtration but only the major form was purified. The pH optimum of the enzyme was 9.5. Exogenous NAD+ was not required for enzymic activity but its removal caused inactivation. The enzyme was unstable below pH 7.0 but stable at pH 8.0 in the presence of glycerol and at −20° for two months. The equilibrium constant for the enzyme-catalysed reaction was 3.2 ± 0.15. The Km for UDP-galactose and UDP-glucose were 0.12 mM and 0.25 mM, respectively. The inhibition by NADH was competitive, with a Ki of 5 μM. The MW of the enzyme was 78 000; the two minor forms showed the values of 158 000 and 39 000, respectively." @default.
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- W1996009886 date "1984-04-01" @default.
- W1996009886 modified "2023-09-23" @default.
- W1996009886 title "UDP-galactose 4′-epimerase from vicia faba seeds" @default.
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- W1996009886 doi "https://doi.org/10.1016/s0031-9422(00)85013-x" @default.
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