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- W2014333559 abstract "UDP–GlcN[1-14C]Ac was synthesized in a single enzymatic reaction from [1-14C]acetate and commercially available precursors on both a microcurie (micromole) and a millicurie (millimole) scale. The reaction was catalyzed by the action of acetyl coenzyme A synthetase, inorganic pyrophosphatase, and the bifunctionalEscherichia coliGlmU protein. Within 2 h 86 to 94% reaction is attained, and it approaches 99% completion overnight. GlmU protein was prepared in the form of a fusion suitable for nickel chelate affinity chromatography. Several methods were developed for rapid purification of UDP–GlcN[1-14C]Ac: an HPLC method handled micromole (microcurie) loads. Alternatively, ion exchange chromatography over DOWEX AG1 X-2 using a batch elution procedure was compatible with millimole (millicurie) amounts of radiolabel and yielded both chemically and radiochemically homogeneous UDP–GlcN[1-14C]Ac. These methods allow laboratories to quickly produce and purify microcurie to millicurie quantities ofN-acetyl-labeled UDP–GlcNAc by a choice of methods from relatively inexpensive precursors." @default.
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- W2014333559 date "1998-02-01" @default.
- W2014333559 modified "2023-09-26" @default.
- W2014333559 title "One-Day Enzymatic Synthesis and Purification of UDP–N- [1-14C]Acetyl-Glucosamine" @default.
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- W2014333559 doi "https://doi.org/10.1006/abio.1997.2525" @default.
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