Linked Life Data

1910387

Source:http://linkedlifedata.com/resource/pubmed/id/1910387

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5-6
pubmed:dateCreated
1991-11-8
pubmed:abstractText
The interaction of the bipyridylium herbicides diquat and paraquat with the proteins gliadin and human serum albumin (HSA) as well as with cellulose and the effect of various ions on the strength of interaction were studied by charge-transfer chromatography. Both compound showed very similar behaviour. The ions decreased in each case the strength of interaction, the effect depended nonlinearly on the ion concentration and was of saturation character. Gliadin showed the weakest interaction. HSA binds the bipyridylium compounds in an ion-dependent manner, the strength of interaction is higher than that of cellulose at higher ion concentration. This finding indicates an ion-mediated interaction of unknown character between the bipyridylium herbicides and HSA.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0939-5075
pubmed:author
pubmed:issnType
Print
pubmed:volume
46
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
428-32
pubmed:dateRevised
2009-11-4
pubmed:meshHeading
pubmed:articleTitle
Ions modify the strength of interaction of diquat and paraquat with some proteins and cellulose.
pubmed:affiliation
Central Research Institute of Chemistry, Hungarian Academy of Sciences, Budapest.
pubmed:publicationType
Journal Article