Linked Life Data

8074803

Source:http://linkedlifedata.com/resource/pubmed/id/8074803

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1994-10-4
pubmed:abstractText
Spodoptera frugiperda cells are the standard host system for baculovirus-vector-mediated expression of recombinant glycoproteins. In an attempt to explore their ability to produce complex N-glycans containing terminal neuraminic acid, we tested both mock- and AcMNPV-infected SF9 cells. To elucidate the structures of the carbohydrate chains of cellular glycoproteins, radiolabeled oligosaccharides were liberated by treatment with endo-H and glycopeptidase F. When the endo-H resistant material was subjected to sequential degradation with exoglycosidases, only truncated carbohydrates with the structures Man3GlcNAc2 and Man3[Fuc]GlcNAc2 were found. There was no evidence for the presence of neuraminic acid and complex N-glycans. The results indicate that SF9 cells have only a limited capacity to process N-glycans. Infection with AcMNPV has no significant effect on glycosylation in these cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0177-3593
pubmed:author
pubmed:issnType
Print
pubmed:volume
375
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
23-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Baculovirus infection does not alter N-glycosylation in Spodoptera frugiperda cells.
pubmed:affiliation
Institut für Virologie, Philipps-Universität, Marburg, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't