Linked Life Data

15533690

Source:http://linkedlifedata.com/resource/pubmed/id/15533690

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2004-11-9
pubmed:abstractText
The interaction between monoammonium glycyrrhizinate (MAG) and bovine serum albumin (BSA) were studied by fluorescence and absorption spectroscopy. The quenching mechanism of fluorescence of bovine serum albumin by monoammonium glycyrrhizinate was discussed. The binding sites number n and apparent binding constant K were measured by fluorescence quenching method. The thermodynamic parameters DeltaH degrees , DeltaG degrees , DeltaS degrees at different temperatures were calculated. The distance r between donor (bovine serum albumin) and acceptor (monoammonium glycyrrhizinate) was obtained according to Forster theory of non-radiation energy transfer. The results of synchronous fluorescence spectra and UV-vis absorption spectra show that the conformation of bovine serum albumin has been changed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0731-7085
pubmed:author
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
36
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
915-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Study of the interaction between monoammonium glycyrrhizinate and bovine serum albumin.
pubmed:affiliation
Department of Chemistry, College of Chemistry and Molecular Sciences, Wuhan University, Wuhan 430072, PR China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't