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Purification and immobilization of acetate kinase from Desulfovibrio vulgaris
Authors:Geert Mannens  Guido Slegers  Albert Claeys
Affiliation:(1) Laboratory of Analytical Chemistry, Faculty of Pharmaceutical Sciences, State University of Ghent, Harelbekestraat 72, B-9000 Ghent, Belgium
Abstract: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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