Abstract
WHEN arylsulphatase (phenolsulphatase) acts on the salt of an arylsulphuric acid (for example, potassium phenylsulphate, C6H5OSO3K), the substrate undergoes hydrolysis. If the phenolic compound liberated on hydrolysis can be converted to a coloured product, the reaction can be made the basis of a method of detecting the enzyme. Earlier workers, using monoarylsulphates prepared from various phenols as substrates for the detection of arylsulphatase, have shown that this enzyme occurs in plants and animals. Its occurrence in bacteria, however, had not been investigated until recently, when Barber, Brooksbank and Kuper1 examined 160 strains of Staphylococcus pyogenes and 75 strains of coagulase-negative staphylococci for the presence of glucuronidase, phosphatase and arylsulphatase, using the monoglucuronide, diphosphate and disulphate of phenolphthalein as substrates. In only two strains of staphylococci was arylsulphatase detected, although the enzyme was found to be present in an aerobic sporing bacillus encountered as a contaminant and in a strain of Salmonella paratyphi B.
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References
Barber, M., Brooksbank, B. W. L., and Kuper, S. W. A., J. Path. Bact., 63, 57 (1951).
Whitehead, J. E. M., Wildy, N. P. L., and Engbaek, H. C. (forthcoming publication).
Evans, W. C., Smith, B. S. W., Linstead, R. P., and Elvidge, J. A., Nature, 168, 772 (1951).
Britton, H. T. S., “Hydrogen Ions” (Chapman and Hall, Ltd., London, 1942).
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YOUNG, L., MORRISON, A. & WHITEHEAD, J. Bacterial Arylsulphatase. Nature 169, 711–712 (1952). https://doi.org/10.1038/169711b0
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DOI: https://doi.org/10.1038/169711b0
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