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dc.contributor.authorBrandan, Enrique
dc.contributor.authorHirschberg, Carlos B.
dc.date2022-08-11T08:10:05.000
dc.date.accessioned2022-08-23T16:54:43Z
dc.date.available2022-08-23T16:54:43Z
dc.date.issued1988-02-15
dc.date.submitted2008-08-15
dc.identifier.citationJ Biol Chem. 1988 Feb 15;263(5):2417-22.
dc.identifier.issn0021-9258 (Print)
dc.identifier.pmid3422231
dc.identifier.urihttp://hdl.handle.net/20.500.14038/42566
dc.description.abstractN-Heparan-sulfate sulfotransferase catalyzes the transfer of sulfate from 3'-phosphoadenilyl sulfate to the nitrogen of glucosamine in heparan sulfate. This reaction is an obligatory step for subsequent epimerization of D-glucuronic to L-iduronic acid and of O-sulfation of the sugar chains. We have purified this sulfotransferase from rat liver membranes to apparent homogeneity using a combination of conventional and affinity chromatography on DEAE-Sephacel, heparin-agarose, 3',5'-ADP-agarose, wheat germ-Sepharose, and finally a glycerol gradient. The pure enzyme is a glycoprotein with an apparent molecular weight of 97,000. It was enriched in specific activity 65,000-fold over the homogenate. The recovery of activity was 4% of that of the homogenate. Preliminary enzymatic characterization of the purified sulfotransferase indicates a high degree of substrate specificity. Transfer of sulfate occurs to heparan sulfate, N-heparan sulfate, and N-desulfated heparin, but not to N-acetylated heparan sulfate, N-acetylated heparin, chondroitin, chondroitin sulfate, and tyrosine-containing tripeptides.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=3422231&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://www.jbc.org/content/263/5/2417.full.pdf+html
dc.subjectAnimals
dc.subjectChromatography, Affinity
dc.subjectChromatography, Gel
dc.subjectElectrophoresis, Polyacrylamide Gel
dc.subjectGolgi Apparatus
dc.subjectLiver
dc.subjectMembranes
dc.subjectRats
dc.subject*Sulfotransferases
dc.subjectSulfurtransferases
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titlePurification of rat liver N-heparan-sulfate sulfotransferase
dc.typeJournal Article
dc.source.journaltitleThe Journal of biological chemistry
dc.source.volume263
dc.source.issue5
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/902
dc.identifier.contextkey579791
html.description.abstract<p>N-Heparan-sulfate sulfotransferase catalyzes the transfer of sulfate from 3'-phosphoadenilyl sulfate to the nitrogen of glucosamine in heparan sulfate. This reaction is an obligatory step for subsequent epimerization of D-glucuronic to L-iduronic acid and of O-sulfation of the sugar chains. We have purified this sulfotransferase from rat liver membranes to apparent homogeneity using a combination of conventional and affinity chromatography on DEAE-Sephacel, heparin-agarose, 3',5'-ADP-agarose, wheat germ-Sepharose, and finally a glycerol gradient. The pure enzyme is a glycoprotein with an apparent molecular weight of 97,000. It was enriched in specific activity 65,000-fold over the homogenate. The recovery of activity was 4% of that of the homogenate. Preliminary enzymatic characterization of the purified sulfotransferase indicates a high degree of substrate specificity. Transfer of sulfate occurs to heparan sulfate, N-heparan sulfate, and N-desulfated heparin, but not to N-acetylated heparan sulfate, N-acetylated heparin, chondroitin, chondroitin sulfate, and tyrosine-containing tripeptides.</p>
dc.identifier.submissionpathoapubs/902
dc.contributor.departmentDepartment of Biochemistry
dc.source.pages2417-22


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