Show simple item record

dc.contributor.authorMandon, Elisabet C.
dc.contributor.authorKempner, Ellis S.
dc.contributor.authorIshihara, Masayuki
dc.contributor.authorHirschberg, Carlos B.
dc.date2022-08-11T08:10:04.000
dc.date.accessioned2022-08-23T16:54:20Z
dc.date.available2022-08-23T16:54:20Z
dc.date.issued1994-04-22
dc.date.submitted2008-08-15
dc.identifier.citationJ Biol Chem. 1994 Apr 22;269(16):11729-33.
dc.identifier.issn0021-9258 (Print)
dc.identifier.pmid8163470
dc.identifier.urihttp://hdl.handle.net/20.500.14038/42476
dc.description.abstractRecent studies have shown that the rat liver heparan sulfate N-deacetylase/N-sulfotransferase is a glycoprotein encoded by a single polypeptide chain of 882 amino acids. Using radiation inactivation analyses, we have now determined that in rat liver Golgi vesicles the target size for the N-deacetylase is 88 +/- 14 kDa, whereas that of the N-sulfotransferase is 92 +/- 8 kDa. These results, together with previous biochemical and molecular cloning approaches, demonstrate that 1) in rat liver Golgi membranes there exists only on population of molecules expressing both activities, 2) the active protein in the Golgi membrane functions as a monomer, and 3) there is no evidence that a large independent protein acts as a regulator of either activity.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=8163470&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://www.jbc.org/content/269/16/11729.long
dc.subjectAmidohydrolases
dc.subjectAnimals
dc.subjectDose-Response Relationship, Radiation
dc.subjectGolgi Apparatus
dc.subjectHeparitin Sulfate
dc.subjectIntracellular Membranes
dc.subjectKinetics
dc.subjectLiver
dc.subjectMolecular Weight
dc.subjectRats
dc.subjectSulfotransferases
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleA monomeric protein in the Golgi membrane catalyzes both N-deacetylation and N-sulfation of heparan sulfate
dc.typeJournal Article
dc.source.journaltitleThe Journal of biological chemistry
dc.source.volume269
dc.source.issue16
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/821
dc.identifier.contextkey579707
html.description.abstract<p>Recent studies have shown that the rat liver heparan sulfate N-deacetylase/N-sulfotransferase is a glycoprotein encoded by a single polypeptide chain of 882 amino acids. Using radiation inactivation analyses, we have now determined that in rat liver Golgi vesicles the target size for the N-deacetylase is 88 +/- 14 kDa, whereas that of the N-sulfotransferase is 92 +/- 8 kDa. These results, together with previous biochemical and molecular cloning approaches, demonstrate that 1) in rat liver Golgi membranes there exists only on population of molecules expressing both activities, 2) the active protein in the Golgi membrane functions as a monomer, and 3) there is no evidence that a large independent protein acts as a regulator of either activity.</p>
dc.identifier.submissionpathoapubs/821
dc.contributor.departmentDepartment of Biochemistry and Molecular Biology
dc.source.pages11729-33


This item appears in the following Collection(s)

Show simple item record