The location of the high- and low-affinity bilirubin-binding sites on serum albumin: Ligand-competition analysis investigated by circular dichroism
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22340%2F13%3A43895115" target="_blank" >RIV/60461373:22340/13:43895115 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1016/j.bpc.2013.06.004" target="_blank" >http://dx.doi.org/10.1016/j.bpc.2013.06.004</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.bpc.2013.06.004" target="_blank" >10.1016/j.bpc.2013.06.004</a>
Alternative languages
Result language
angličtina
Original language name
The location of the high- and low-affinity bilirubin-binding sites on serum albumin: Ligand-competition analysis investigated by circular dichroism
Original language description
The locations of three bilirubin (BR)-binding sites with different affinities were identified as subdomains IB, IIA and IIIA for five mammalian serum albumins (SAs): human (HSA), bovine (BSA), rat, (RSA), rabbit (RbSA) and sheep (SSA). The stereoselectivity of a high-affinity BR-binding site was identified in the BR/SA=1/1 system by circular dichroism (CD) spectroscopy, the sites with low affinity to BR were analyzed using difference CD. Site-specific ligand-competition experiments with ibuprofen (marker for subdomain IIIA) and hemin (marker for subdomain IB) did not reveal any changes for the BR/SA=1/1 system and showed a decrease of the bound BR at BR/SA=3/1. Both sites were identified as sites with low affinity to BR. The correlation between stereoselectivity and the arrangement of Arg-Lys residues indicated similarity between the BR-binding sites in subdomain IIIA for all of the SAs studied. Subdomain IB in HSA, BSA, SSA and RbSA has P-stereoselectivity while in RSA it has M-select
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CB - Analytical chemistry, separation
OECD FORD branch
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Result continuities
Project
<a href="/en/project/GAP206%2F11%2F0836" target="_blank" >GAP206/11/0836: Structural Study of Potentially Bioactive Bile Pigment Complexes: Relation to their Protective Function in Organisms</a><br>
Continuities
S - Specificky vyzkum na vysokych skolach
Others
Publication year
2013
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Biophysical Chemistry
ISSN
1873-4200
e-ISSN
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Volume of the periodical
180-181
Issue of the periodical within the volume
22 June 2013
Country of publishing house
NL - THE KINGDOM OF THE NETHERLANDS
Number of pages
11
Pages from-to
55-65
UT code for WoS article
000324898700007
EID of the result in the Scopus database
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