Linked Life Data

6420399

Source:http://linkedlifedata.com/resource/pubmed/id/6420399

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1984-3-5
pubmed:abstractText
The effects of ligand binding on antibody complex formation of Lactobacillus casei dihydrofolate reductase have been investigated. Binary complexes containing either substrate and inhibitors or NADP+ and NADPH together with ternary complexes containing inhibitors and coenzyme were examined. Whereas substrate and inhibitor binding alone show no effect, the binding of coenzyme reduces antibody complex formation. The most striking effect is observed with ternary complexes containing methotrexate or aminopterin and NADPH: maximal retention of the labeled protein in the immunoprecipitation assay is reduced to approximately 30% of its original value with dihydrofolate reductase alone due to a decrease in both the affinity and lifetime of the antibody-protein complex at one or more antigenic sites. This result is discussed in terms of different conformational changes brought about by NADP and NADPH.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
259
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1082-5
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Immunochemical evidence for extensive ligand-induced conformational changes in Lactobacillus casei dihydrofolate reductase.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't