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. 1982 Feb 1;201(2):345–352. doi: 10.1042/bj2010345

The slow kinetic transients of arylsulphatase A.

C O'Fagain, U Bond, B A Orsi, T J Mantle
PMCID: PMC1163649  PMID: 6123317

Abstract

A simple model is described to account for the anomalous time course of arylsulphatase A. In the case of the ox liver and human placental enzymes the enzyme-nitrocatechol sulphate complex can, in addition to forming products, slowly break down to form an inactive species which can turn in slowly regenerate active enzyme. When the inactive form binds sulphate the rate of reactivation is enhanced, 218-fold in the case of the ox enzyme. Rat liver arylsulphatase A is refractory to reactivation by sulphate.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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