Linked Life Data

7308392

Source:http://linkedlifedata.com/resource/pubmed/id/7308392

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1982-2-12
pubmed:abstractText
The affinity between purified rheumatoid factors (RF) and native or heat aggregated human IgG has been studied in vitro by polarization fluorescence in the presence and in the absence of D-penicillamine. The value of the dissociation constant was the same using native and heat aggregated IgG suggesting that binding to the aggregated protein is not dependent on the exposure of a new determinant lacking in the native molecule. The results obtained in the presence of D-penicillamine suggest that the concentration of the drug necessary to get a pronounced effect on the apparent dissociation constant of the immunocomplex between IgG and RF is not reached in vivo, in clinical situations.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0014-4754
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
37
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1070-1
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Action of D-penicillamine on immunocomplexes containing rheumatoid factor.
pubmed:publicationType
Journal Article, Comparative Study, In Vitro