Linked Life Data

1482374

Source:http://linkedlifedata.com/resource/pubmed/id/1482374

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1993-2-8
pubmed:abstractText
Recombinant human tissue plasminogen activator expressed in murine epithelial cells carries, in part, sulfated N-glycans, which are characterized by the presence of a NeuAc alpha 3[SO4-6]Gal unit. In order to study the biosynthesis of this novel structural element, corresponding sulfated asialooligosaccharide alditols were resialylated in vitro using a crude sialyltransferase preparation from murine liver which was shown to contain Gal beta 1,3(4)GlcNAc alpha 2,3-sialyltransferase activity. Products were analyzed for transfer of sialic acid residues by anion-exchange HPLC. The results demonstrated that resialylation of SO4-6Gal-residues did not occur. Therefore, it may be concluded that transfer of the sulfate group is the final step in the biosynthesis of this structural epitope.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
189
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1681-5
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Biosynthesis of sulfated glycoprotein-N-glycans present in recombinant human tissue plasminogen activator.
pubmed:affiliation
Institute of Biochemistry, University of Giessen, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't