Linked Life Data

19139584

Source:http://linkedlifedata.com/resource/pubmed/id/19139584

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2009-1-13
pubmed:abstractText
Two fluorescence modes were combined to analyze the binding properties of terminally substituted alkanes (C(n)X, X = COOH, OH, CHO, NH(2)) to human serum albumin (HSA). A competitive binding assay using an 8-anilino-1-naphthalenesulfonate (ANS) fluorescence probe provides information on all the hydrophobic binding sites in HSA. A binding assay using the intrinsic fluorescence of the tryptophan residue in HSA (Trp-HSA) provides information on the specific binding site close to the tryptophan residue. There are three fluorescence-active ANS binding sites in HSA, which can be classified into two types by their affinity for ANS. C(n)COOH bound to all three ANS binding sites including the Trp-HSA site, however, it did not quench the fluorescence of Trp-HSA. C(n)CHO bound only to the Trp-HSA site with quenching of the fluorescence of Trp-HSA. By comparing the binding affinities of HSA for C(n)OH and C(n)CHO, it was concluded that the C(n)OH binding site is different from the C(n)CHO binding site. C(n)NH(2) did not bind to any of the three ANS binding sites in HSA.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1348-2246
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
25
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
115-20
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Binding properties of hydrophobic molecules to human serum albumin studied by fluorescence titration.
pubmed:affiliation
Department of Chemistry, Faculty of Sciences, Kyushu University, Fukuoka 810-8560, Japan. kou@rc.kyushu-u.ac.jp
pubmed:publicationType
Journal Article