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Purification and properties of a second enzyme catalyzing the splitting of carbon-mercury linkages from mercury-resistant Pseudomonas K-62
- Source :
- Journal of Bacteriology; July 1978, Vol. 135 Issue: 1 p138-143, 6p
- Publication Year :
- 1978
-
Abstract
- An enzyme (splitting enzyme 2) which catalyzes the splitting of carbon-mercury linkage of arylmercury compounds was found in extracts of mercury-resistant Pseudomonas K-62. This enzyme was purified about 725-fold by treatment with streptomycin, precipitation with ammonium sulfate, and successive chromatography on Sephadex G-75 and diethylaminoethyl-cellulose. A purified preparation of the enzyme showed a single band in electrophoresis either on polyacrylamide or sodium dodecyl sulfate-containing polyacrylamide gels. The molecular weight of the enzyme was estimated to be 20,000 (determined by Sephadex G-75 gel filtration) 17,000 (determined by sodium dodecyl sulfate-polyacrylamide disc gel electrophoresis). The enzyme showed a Km of 180 micron and a Vmax of 3.1 mumol/min per mg for p-chloromercuribenzoic acid and a Km of 250 micron and a Vmax of 20 mumol/min per mg for phenylmercuric acetate. The optimum temperature and pH for the reaction were 40 degrees C and 5.0, respectively.
Details
- Language :
- English
- ISSN :
- 00219193 and 10985530
- Volume :
- 135
- Issue :
- 1
- Database :
- Supplemental Index
- Journal :
- Journal of Bacteriology
- Publication Type :
- Periodical
- Accession number :
- ejs57599548
- Full Text :
- https://doi.org/10.1128/jb.135.1.138-143.1978