Linked Life Data

17112044

Source:http://linkedlifedata.com/resource/pubmed/id/17112044

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2006-11-20
pubmed:abstractText
The interaction of quercetin and bovine serum albumin (BSA) was investigated using fluorescence spectroscopy (FS) and ultraviolet spectroscopy (UV). The apparent binding constants (KA) between quercetin and BSA were 2.8 x 10(8) (26 degrees C) and 3.1 x 10(8) (36 degrees C), and the binding sites (n) were 1.7+/-0.02. According to the Förster theory of non-radiation energy transfer, the binding distances (r) were also obtained. The experimental results showed that the quercetin could be inserted into the BSA, quenching the inner fluorescence by forming the quercetin-BSA complex. It was found that both static quenching and non-radiation energy transfer were the main reasons for the fluorescence quenching. The process of binding was a spontaneous molecular interactioln in which entropy increased while Gibbs free energy decreased, indicating that the interaction of quercetin and BSA was driven mainly by hydrophobic force.
pubmed:language
chi
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1000-0593
pubmed:author
pubmed:issnType
Print
pubmed:volume
26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1672-5
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
[Interaction of quercetin and bovine serum albumin].
pubmed:affiliation
College of Sciences, Agricultural University of Hebei, Baoding 071001, China.
pubmed:publicationType
Journal Article, English Abstract