|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
5
|
|
pubmed:dateCreated |
1993-8-26
|
|
pubmed:abstractText |
The precise nature of the epitope on the Fc portion of the IgG molecule to which IgG rheumatoid factors (RF) bind has not been identified. As patients with rheumatoid arthritis (RA) have abnormal glycosylation of the Fc portion of IgG, we investigated the impact of the sugar present in the Fc on the binding of IgG RF.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
May
|
|
pubmed:issn |
0315-162X
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
20
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
776-80
|
|
pubmed:dateRevised |
2010-3-24
|
|
pubmed:meshHeading |
|
|
pubmed:year |
1993
|
|
pubmed:articleTitle |
Binding of human monoclonal IgG rheumatoid factors to Fc is influenced by carbohydrate.
|
|
pubmed:affiliation |
Department of Medicine, McGill University, Montreal General Hospital Research Institute, PQ, Canada.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
