| Literature DB >> 16503297 |
Kanako Tago1, Sumiko Yonezawa, Toshihide Ohkouchi, Masayuki Hashimoto, Masahito Hayatsu.
Abstract
The organophosphorus pesticide hydrolase was purified to homogeneity from Burkholderia sp. NF100 by detergent extraction of the cell membrane fraction, anion-exchange, chromatofocusing, and gel filtration chromatographies. The purified enzyme had a molecular mass of 55 kDa and a pI 5.8, and the hydrolase activity was strongly inhibited by EDTA, dithiothreitol (DTT), Hg2+ and 1,10-phenanthroline. The optimum pH and temperature for the enzyme activity were 8.0 and 40 degrees C, respectively. The enzyme hydrolyzed five organophosphorus pesticides.Entities:
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Year: 2006 PMID: 16503297 DOI: 10.1263/jbb.101.80
Source DB: PubMed Journal: J Biosci Bioeng ISSN: 1347-4421 Impact factor: 2.894