Abstract.
N-acetyltransferase from Aeromonas hydrophilia was purified by ultrafiltration, DEAE-Sephacel, gel filtration chromatography on Sephadex G-100, and DEAE-5pw on high performance liquid chromatography, as judged by sodium dodecyl sulfate-polyacrylamine gel electrophoresis (SDS-PAGE) on a 12.% (wt/vol) slab gel. The enzyme had a molecular mass 44.9 kDa. The purified enzyme was thermostable at 37°C for 1 h with a half-life 28 min at 37°C, and displayed optimum activity at 37°C and pH 7.0. The K m and V max values for 2-aminofluorene were determined to be 0.896 mM and 2.456 nmol/min/mg protein, respectively. Among a series of divalent cations and salts, Zn2+, Ca2+, and Fe2+ were demonstrated to be the most potent inhibitors.
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Received: 10 November 1997 / Accepted: 17 February 1998
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Chung, J. Purification and Characterization of an Arylamine N-Acetyltransferase from the Bacteria Aeromonas hydrophilia . Curr Microbiol 37, 70–73 (1998). https://doi.org/10.1007/s002849900341
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DOI: https://doi.org/10.1007/s002849900341