Summary
The enzyme acetate kinase (EC 2.7.2.1) was purified fromDesulfovibrio vulgaris by a combination of ammonium sulfate precipitation, hydroxyl-apatite and dye-affinity chromatography. An overall-purification factor of 15 was obtained resulting in a specific activity of 24 U/mg protein. The purified enzyme was immobilized on differently derivatized controlled pore glass beads.
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Mannens, G., Slegers, G. & Claeys, A. Purification and immobilization of acetate kinase from Desulfovibrio vulgaris. Biotechnol Lett 10, 563–568 (1988). https://doi.org/10.1007/BF01027130
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DOI: https://doi.org/10.1007/BF01027130