Properties and sub-cellular distribution of two sulfatases which degrade adenosine 5′-phosphosulfate

Donald Armstrong*, James Austin, Thomas Luttenegger, Bimal Bachhawat, David Stumpf

*Corresponding author for this work

Research output: Contribution to journalArticle

13 Scopus citations

Abstract

Adenosine 5′-phosphosulfate (APS)-sulfatase splits sulfate from APS, the direct precursor of 3t́-phosphoadenosine 5′-phosphosulfate (PAPS) "active sulfate". The properties and sub-cellular distribution of APS-sulfatase activity are described in pig kidney cortex. The evidence is consistent with the existence of two species of APS-sulfatases. One enzyme species has an acid and the other a neutral pH optimum. The two differ in their electrophoretic distribution patterns. Activities are concentrated in the vesicles of the smooth endoplasmic reticulum (smooth-4 fraction), in lysosomes, and in the nuclear fraction. Km values indicate a high affinity of these enzymes for APS. APS-sulfatases were also studied in the human and in the rat. The position of these APS-sulfatases in the pathways of sulfate metabolism suggests that they may play an important role in governing sulfate conjugation from PAPS.

Original languageEnglish (US)
Pages (from-to)523-537
Number of pages15
JournalBBA - Enzymology
Volume198
Issue number3
DOIs
StatePublished - Mar 18 1970

ASJC Scopus subject areas

  • Medicine(all)

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