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Assay of sulfotransferases

Authors
Journal
Analytical Biochemistry
0003-2697
Publisher
Elsevier
Volume
95
Issue
1
Identifiers
DOI: 10.1016/0003-2697(79)90188-x
Keywords
  • Enzymatic Assays And Analyses
Disciplines
  • Biology

Abstract

Abstract Two methods are described for the assay of sulfotransferases which are active with sulfate acceptors bearing the hydroxyl functional group. Assays were developed for enzymes which transfer sulfate from 3′-phosphoadenosine–5′-phosphosulfate (PAPS) to sterols, phenols, and simple alcohols thereby forming the corresponding sulfate esters. With a filter binding assay, useful with crude and purified enzyme preparations, a radioactive sterol substrate is used and subsequently separated from labeled product, allowing the determination of between 50 and 400 pmol of product. In a second method, [35S]PAPS is used and the labeled product is separated from PAPS and inorganic sulfate by a thin-layer technique in which product migrates close to the solvent front; the assay is useful with a broad array of substrates and is more sensitive than the filter binding assay.

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