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. 1971 Aug;123(5):901–906. doi: 10.1042/bj1230901

Purification from rat liver of an enzyme that catalyses the sulphurylation of phenols

F A McEvoy 1, J Carroll 1
PMCID: PMC1177091  PMID: 5124393

Abstract

1. An enzyme (EC 2.8.2.1) that catalyses the transfer of sulphate from adenosine 3′-phosphate 5′-sulphatophosphate to phenols was purified approx. 2000-fold from male rat livers. 2. The purified preparation did not catalyse the sulphurylation of dehydroepiandrosterone, butan-1-ol, l-tyrosine methyl ester, 1-naphthylamine or serotonin. 3. At pH8.0 and 37°C the Km values of the enzyme for p-nitrophenol and adenosine 3′-phosphate 5′-sulphatophosphate are 51 and 14μm respectively. The Km value for either substrate is independent of the concentration of the other. 4. The sulphurylation of phenol is inhibited by thiol compounds and glutathione at a concentration of 3mm caused an approx. 50% decrease in enzyme activity. 5. The Km of the enzyme for adenosine 3′-phosphate 5′-sulphatophosphate is unaffected by the presence of added glutathione but at a concentration of 5mm-glutathione the Km of the enzyme for its phenolic substrate is decreased.

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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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