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Rapid purification method for human recombinant tumor necrosis factor alpha.

A Paquet·A Lévesque·M Pagé
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Abstract

Human recombinant tumor necrosis factor alpha was purified in a single step to about 95% purity from Escherichia coli lysate by chromatography on hydroxyapatite. The last traces of contaminants were removed by fast protein liquid chromatography on a Mono Q column. The final product was found to be pure by gel electrophoresis with silver staining. A molecular mass of approximately 17,000 and a specific activity of 4.3 x 10(6) U/mg after a single purification step were found.

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Amino AcidsAnion Exchange ResinsChromatography, LiquidElectrophoresis, Polyacrylamide GelEscherichia coliHumansHydroxyapatitesMolecular WeightRecombinant ProteinsResins, SyntheticSpectrophotometry, UltravioletTumor Necrosis Factor-alphaJournal Article

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BibTeXRIS

A Paquet, A Lévesque, M Pagé. 1994-04-29. Rapid purification method for human recombinant tumor necrosis factor alpha.. https://doi.org/10.1016/0021-9673(94)89060-9

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