Measurement of nucleoside diphosphate kinase-Nm23 activity by anion-exchange high-performance liquid chromatography
| Autor: | James Gordon, Gabriel Pulido-Cejudo, Jose Campione-Piccardo, Josée Gagnon, Keri Jamison, Jean-Marie Leclerc |
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| Rok vydání: | 1994 |
| Předmět: |
Ribonucleotide
Ion chromatography High-performance liquid chromatography Phosphates chemistry.chemical_compound Cytosol Tumor Cells Cultured Animals Humans Chromatography High Pressure Liquid chemistry.chemical_classification Chromatography biology Substrate (chemistry) General Chemistry Ribonucleotides Phosphate Chromatography Ion Exchange Enzyme assay Nucleoside-diphosphate kinase Neoplasm Proteins Kinetics Enzyme chemistry Liver Nucleoside-Diphosphate Kinase biology.protein Cattle Guanosine Triphosphate |
| Zdroj: | Journal of chromatography. B, Biomedical applications. 660(1) |
| ISSN: | 1572-6495 |
| Popis: | A first-order assay to detect the activity of nucleoside diphosphate kinase (NDP-kinase; EC 2.7.4.6) was developed. In this assay, the activity of NDP-kinase is measured using various deoxy- and ribonucleotide triphosphates as phosphate donors and dADP as phosphate acceptor. The enzyme activity is determined by quantifying, after anion-exchange HPLC, the amount of newly synthesized dATP. Contrary to the most common coupled enzymic assays or isotopic assays the use of different donor—acceptor pairs is not restricted. The resolution of the procedure described is limited only by the chromatographic separation of substrate and product pairs participating in the reaction. |
| Databáze: | OpenAIRE |
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