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PMID: 1200998 Published · ppublish English Journal Article

Studies on the Arylsulphatase and phenol sulphotransferase activities of Aspergillus oryzae.

The Biochemical journal ·Vol. 149 ·No. 3 ·1975-09-00 ·Pages 697-705

Burns GR, Wynn CH

Abstract

1. Crude extracts of Aspergillus oryzae grown under conditions of sulphur limitation possess high arylsulphatase activity. 2. This activity can be greatly enhanced by the inclusion of tyramine or a number of other phenols in the assay medium. 3. The arylsulphatase activity of these extracts can be resolved into three distinct fractions by chromatography on DEAE-cellulose. 4. The effect of tyramine is restricted to one of these fractions only. 5. Evidence is presented which indicates that this effect is the consequence of a phenol sulphotransferase activity, which shows no requirement for 3'-phosphoadenosine 5'-phosphate as a cofactor, and which will not transfer sulphate from 3'-phosphoadenosine 5'-sulphatophosphate to potential phenolic acceptors. 6. The three enzymes differ also in their molecular weights and substrate specificities.

MeSH Terms
Arylsulfatases/metabolism Aspergillus/enzymology Aspergillus oryzae/enzymology Chromatography, DEAE-Cellulose Chromatography, Gel Chromatography, Thin Layer Kinetics Molecular Weight Phenols/pharmacology Phosphoadenosine Phosphosulfate/metabolism Sulfatases/metabolism Sulfurtransferases/metabolism Tyramine/pharmacology
Chemicals
Phenols Phosphoadenosine Phosphosulfate Sulfurtransferases Sulfatases Arylsulfatases Tyramine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Burns G R
Wynn C H
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24 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj1490697
Published
1975-09-00
Pages
697-705
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1165676
Subset
IM
External Links
PubMed source DOI: 10.1042/bj1490697 PMC Full Text View journal details
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