Linked Life Data

21345721

Source:http://linkedlifedata.com/resource/pubmed/id/21345721

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2011-3-28
pubmed:abstractText
The interaction between salvianic acid A sodium (SAS) and bovine serum albumin (BSA) was investigated using fluorescence and ultraviolet spectroscopy at different temperatures under imitated physiological conditions. The experimental results showed that the fluorescence of BSA was quenched by SAS through a static quenching procedure. The binding constants of SAS with BSA were 2.03, 1.17 and 0.71×10(5) L mol(-1) at 291, 298 and 305 K, respectively. Negative values of ?G, ?H, and ?S indicate that the interaction between SAS and BSA is driven by hydrogen bonds and van der Waals forces. According to Förster non-radiation energy transfer theory, the binding distance between BSA and SAS was calculated to be about 2.92 nm. The effect of SAS on the conformation of BSA was analyzed using synchronous fluorescence spectroscopy. In addition, the effect of some metal ions Cu(2+), Ca(2+), Mg(2+), and Zn(2+) on the binding constant between SAS and BSA was examined.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1873-3557
pubmed:author
pubmed:copyrightInfo
Copyright © 2011 Elsevier B.V. All rights reserved.
pubmed:issnType
Electronic
pubmed:volume
78
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1535-9
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Study on the interaction between salvianic acid A sodium and bovine serum albumin by spectroscopic methods.
pubmed:affiliation
Key Laboratory of Theoretical Chemistry and Molecular Simulation of Ministry of Education, School of Chemistry and Chemical Engineering, Hunan University of Science and Technology, Xiangtan, China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't