The location of the high- and low-affinity bilirubin-binding sites on serum albumin: Ligand-competition analysis investigated by circular dichroism

Kód výsledku v 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>

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

The location of the high- and low-affinity bilirubin-binding sites on serum albumin: Ligand-competition analysis investigated by circular dichroism

Popis výsledku v původním jazyce

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

Název v anglickém jazyce

The location of the high- and low-affinity bilirubin-binding sites on serum albumin: Ligand-competition analysis investigated by circular dichroism

Popis výsledku anglicky

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

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CB - Analytická chemie, separace

OECD FORD obor

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Projekt

<a href="/cs/project/GAP206%2F11%2F0836" target="_blank" >GAP206/11/0836: Strukturní studie potencionálně bioaktivních komplexů žlučových barviv: Vztak k jejich ochranné funkci v organismech</a><br>

Návaznosti

S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2013

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Biophysical Chemistry

ISSN

1873-4200

e-ISSN

—

Svazek periodika

180-181

Číslo periodika v rámci svazku

22 June 2013

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

11

Strana od-do

55-65

Kód UT WoS článku

000324898700007

EID výsledku v databázi Scopus

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