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. 1973 Sep;135(1):187–192. doi: 10.1042/bj1350187

Heparan sulphate sulphotransferase. Properties of an enzyme from ox lung

T Foley 1,*, J R Baker 1,*
PMCID: PMC1165803  PMID: 4798179

Abstract

A heparan sulphate sulphotransferase was partially purified from an ox lung homogenate by (NH4)2SO4 precipitation. Various glycosaminoglycans were assayed as sulphate acceptors with this enzyme. The highest acceptor activity was obtained with desulphated heparin and heparan sulphate, which indicates that sulphate transfer may be to free amino groups of the substrate. Some heparan sulphate was 35S-labelled by incubation with the enzyme and re-isolated. On treatment of this heparan [35S]sulphate with nitrous acid and separation of the degradation products on Sephadex G-15, a major peak of radioactivity was obtained, and identified as [35S]sulphate by high-voltage electrophoresis at pH5.3. The [35S]sulphate is believed to be derived from N-[35S]sulphated groups of heparan [35S]-sulphate. That the ox lung preparation contained an N-sulphotransferase was confirmed by the isolation of 2-deoxy-2-[35S]sulphoamino-d-glucose as the major product from the flavobacterial degradation of heparan [35S]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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