Show simple item record

dc.contributor.authorShen, Yanqinen_US
dc.contributor.authorTiralongo, Joeen_US
dc.contributor.authorIwersen, Matthiasen_US
dc.contributor.authorSipos, Benceen_US
dc.contributor.authorKalthoff, Holgeren_US
dc.contributor.authorSchauer, Rolanden_US
dc.date.accessioned2017-05-03T14:17:02Z
dc.date.available2017-05-03T14:17:02Z
dc.date.issued2002en_US
dc.date.modified2008-02-14T08:10:17Z
dc.identifier.issn1431-6730en_US
dc.identifier.urihttp://hdl.handle.net/10072/16677
dc.description.abstractSialic acids present on human colonic mucins are highly O-acetylated, however, little is known about the underlying enzymatic activity required for O-acetylation in this tissue. Here we report on the substrate specificity, subcellular localization and characterization of the sialate-7(9)-O-acetyltransferase in normal human colonic mucosa. Using CMP-Neu5Ac, the most efficient acceptor substrate of all those tested, the enzymatic activity was found to be optimal at 37 ì with a pH optimum of 7.0. Activity was also found to be dependent on protein, CMP-Neu5Ac (Km: 59.2 卩 and AcCoA (Km: 6.1 卩 concentrations, as well as membrane integrity. The enzyme's activity could be inhibited by CoA with a Ki of 11.9 卮 In addition, enzymatic activity was found to be localized in the Golgi-enriched membrane fraction. The nature of the O-acetylated products formed were verified with the aid of chromatographic and enzymatic techniques. The main product was 9-O-acetylated Neu5Ac, with a significant amount of oligo-O-acetylated Neu5Ac also being detected. The utilization of CMP-Neu5Ac as the acceptor substrate was confirmed by the isolation and characterization of the putative product, CMP-Neu5,9Ac2, using ion-exchange chromatography. The ability of CMP-Neu5,9Ac2 to act as a sialic acid donor for sialyltransferases represents the conclusive demonstration for the formation of CMP-Neu5,9Ac2.en_US
dc.description.peerreviewedYesen_US
dc.description.publicationstatusYesen_AU
dc.languageEnglishen_US
dc.language.isoen_AU
dc.publisherWalter de Gruyteren_US
dc.publisher.placeGermanyen_US
dc.relation.ispartofpagefrom307en_US
dc.relation.ispartofpageto317en_US
dc.relation.ispartofjournalBiological Chemistryen_US
dc.relation.ispartofvolume383en_US
dc.subject.fieldofresearchcode320302en_US
dc.subject.fieldofresearchcode270108en_US
dc.titleCharacterization of the sialate-7(9)-O-acetyltransferase from the microsomes of human colonic mucosaen_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
gro.date.issued2002
gro.hasfulltextNo Full Text


Files in this item

FilesSizeFormatView

There are no files associated with this item.

This item appears in the following Collection(s)

  • Journal articles
    Contains articles published by Griffith authors in scholarly journals.

Show simple item record