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. 2010 Jun 7;285(32):24825–24833. doi: 10.1074/jbc.M110.125872

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FIGURE 2. — Expression and characterization of recombinant UGlcNAcDH. A, SDS-PAGE of total soluble protein isolated from E. coli cells expressing UGlcNAcDH (lane 1) or control empty vector (lane 2) and of nickel column-purified fractions (lane 3, UGlcNAcDH; lane 4, control). B, high pressure liquid chromatogram of UGlcNAcDH enzyme reaction. Purified recombinant UGlcNAcDH was incubated with UDP-GlcNAc in the presence (panel 5), or absence (panel 7) of exogenous NAD⁺. As a control, the corresponding column-purified protein isolated from cells expressing control empty vector was incubated with UDP-GlcNAc and NAD⁺ (panel 6). Activity of total protein isolated from cells expressing recombinant UGlcNAcDH or vector control is shown in panel 2 and 3, respectively. The reaction products were separated on a Q15 column, and the UDP-sugar peak (marked by arrow, in panels 2 and 5) were collected and analyzed by MALDI-MS and NMR.