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dc.contributor.authorTiralongo, E
dc.contributor.authorSchrader, S
dc.contributor.authorLange, H
dc.contributor.authorLemke, H
dc.contributor.authorTiralongo, J
dc.contributor.authorSchauer, R
dc.date.accessioned2017-05-03T14:35:19Z
dc.date.available2017-05-03T14:35:19Z
dc.date.issued2003
dc.date.modified2009-02-27T06:45:26Z
dc.identifier.issn0021-9258
dc.identifier.doi10.1074/jbc.M212909200
dc.identifier.urihttp://hdl.handle.net/10072/21421
dc.description.abstractTrypanosomes express an enzyme called trans-sialidase (TS), which enables the parasites to transfer sialic acids from the environment onto trypanosomal surface molecules. Here we describe the purification and characterization of two TS forms from the African trypanosome Trypanosoma congolense. The purification of the two TS forms using a combination of anion exchange chromatography, isoelectric focusing, gel filtration, and subsequently, antibody affinity chromatography resulted, in both cases, in the isolation of a 90-kDa monomer on SDS-PAGE, which was identified as trans-sialidase using micro-sequencing. Monoclonal antibody 7/23, which bound and partially inhibited TS activity, was found in both cases to bind to a 90-kDa protein. Both TS forms possessed sialidase and transfer activity, but markedly differed in their activity ratios. The TS form with a high transfer-to-sialidase activity ratio, referred to as TS-form 1, possessed a pI of pH 4-5 and a molecular mass of 350-600 kDa. In contrast, the form with a low transfer-to-sialidase activity ratio, referred to as TS-form 2, exhibited a pI of pH 5-6.5 and a molecular mass of 130-180 kDa. Both TS forms were not significantly inhibited by known sialidase inhibitors and revealed no significant differences in donor and acceptor substrate specificities; however, TS-form 1 utilized various acceptor substrates with a higher catalytic efficiency. Interestingly, glutamic acid-alanine-rich protein, the surface glycoprotein, was co-purified with TS-form 1 suggesting an association between both proteins.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.languageEnglish
dc.language.isoeng
dc.publisherThe American Society for Biochemistry and Molecular Biology
dc.publisher.placeUSA
dc.relation.ispartofpagefrom23301
dc.relation.ispartofpageto23310
dc.relation.ispartofissue26
dc.relation.ispartofjournalJournal of Biological Chemistry
dc.relation.ispartofvolume278
dc.subject.fieldofresearchChemical sciences
dc.subject.fieldofresearchBiological sciences
dc.subject.fieldofresearchBiomedical and clinical sciences
dc.subject.fieldofresearchcode34
dc.subject.fieldofresearchcode31
dc.subject.fieldofresearchcode32
dc.titleTwo Trans-sialidase Forms with Different Sialic Acid Transfer and Sialidase Activities from Trypanosoma congolense
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.date.issued2003
gro.hasfulltextNo Full Text
gro.griffith.authorTiralongo, Evelin
gro.griffith.authorTiralongo, Joe


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