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note
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The enzymatic activity of the GST-Cdc25 recombinant enzyme was performed in 96-well plates in [50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA and 0.1% SAB, pH 8,1] buffer containing 3-O-methylfluorescein phosphate 500 μM as substrate. The Gst-Cdc25 proteins, diluted in assay buffer, were used at a final concentration of 1 μg/well. After 2 h at 30 °C, 3-O-methylfluorescein fluorescent emission was measured with a CytoFluor system Perspective Applied Biosystems; excitation filter: 475 nm and emission filter: 510 nm.
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All compounds were characterized by HRMS (ESI) and NMR analysis
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(a) All compounds were characterized by HRMS (ESI) and NMR analysis.
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