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The Sulphatase of ‘Clarase’: Inhibition, Inactivation and Purification

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Abstract

THE optimal conditions and specificity of the enzyme sulphatase of ‘clarase’ have been described in a previous communication1. The method then used of measuring the activity of the enzyme by the gravimetric estimation of sulphate liberated from the substrate has now been abandoned, and a new colorimetric method adopted. In this the amount of phenol set free from the substrate (potassium phenylsulphate) in the course of enzymic hydrolysis is determined, as was done by King and Armstrong2 for the determination of phosphatase.

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References

  1. Dzialoszynski, L. M., Nature, 180, 464 (1947).

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  2. King, E. T., and Armstrong, A. B., Canad. Med. Assoc. J., 376 (Oct. 1934).

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Authors and Affiliations

  1. Biochemical Laboratory, Organic Chemistry Department, University of Poznan,

    L. M. DZIALOSZYNSKI

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  1. L. M. DZIALOSZYNSKI
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DZIALOSZYNSKI, L. The Sulphatase of ‘Clarase’: Inhibition, Inactivation and Purification. Nature 166, 157–158 (1950). https://doi.org/10.1038/166157b0

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