Linked Life Data

8782411

Source:http://linkedlifedata.com/resource/pubmed/id/8782411

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1997-1-28
pubmed:abstractText
N-Linked oligosaccharides were elongated by glycosylation with mannose and galactose residues in the secretory pathway of Schizosaccharomyces pombe. The wild-type S. pombe cells were agglutinated by the additions of not only concanavalin A lectin, which is specific for mannose residues, but also PNA (from Arachis hypogaea) and RCA (Ricinus communis) lectins, which are specific for terminal galactose residues. By PNA-binding selection, we isolated an S. pombe mutant defective in protein glycosylation. The mutant cells, named gms1, were not agglutinated by PNA or RCA. In contrast, agglutination of the gms1 cells by the addition of concanavalin A was markedly increased. Structural studies on N-linked oligosaccharides from gms1 mutant cells showed that the number of alpha-1,2-linked galactose residues wes markedly reduced, and unsubstituted alpha-1,6-linked polymannose outer chains were attached to the core oligosaccharides.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
B
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0916-8451
pubmed:author
pubmed:issnType
Print
pubmed:volume
60
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1156-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Isolation and characterization of a glycosylation mutant from Schizosaccharomyces pombe.
pubmed:affiliation
Department of Bioresource Science, Faculty of Agriculture, Kagawa University, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't