Photo-isomerization and oxidation of bilirubin in mammals is dependent on albumin binding
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11110%2F15%3A10312700" target="_blank" >RIV/00216208:11110/15:10312700 - isvavai.cz</a>
Alternative codes found
RIV/60461373:22340/15:43900288
Result on the web
<a href="http://dx.doi.org/10.1016/j.ab.2015.08.001" target="_blank" >http://dx.doi.org/10.1016/j.ab.2015.08.001</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.ab.2015.08.001" target="_blank" >10.1016/j.ab.2015.08.001</a>
Alternative languages
Result language
angličtina
Original language name
Photo-isomerization and oxidation of bilirubin in mammals is dependent on albumin binding
Original language description
The bilirubin (BR) photo-conversion in the human body is a protein-dependent process; an effective photo-isomerization of the potentially neurotoxic Z,Z-BR as well as its oxidation to biliverdin in the antioxidant redox cycle is possible only when BR isbound on serum albumin. We present a novel analytical concept in the study of linear tetrapyrroles metabolic processes based on an in-depth mapping of binding sites in the structure of human serum albumin (HSA). A combination of fluorescence spectroscopy, circular dichroism (CD) spectroscopy, and molecular modeling methods was used for recognition of the binding site for BR, its derivatives (mesobilirubin and bilirubin ditaurate), and the products of the photo-isomerization and oxidation (lumirubin, biliverdin, and xanthobilirubic acid) on HSA. The CD spectra and fluorescent quenching of the Trp-HSA were used to calculate the binding constants. The results of the CD displacement experiments performed with hemin were interpreted together
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
CE - Biochemistry
OECD FORD branch
—
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
2015
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Analytical Biochemistry
ISSN
0003-2697
e-ISSN
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Volume of the periodical
490
Issue of the periodical within the volume
December
Country of publishing house
US - UNITED STATES
Number of pages
12
Pages from-to
34-45
UT code for WoS article
000363360500006
EID of the result in the Scopus database
2-s2.0-84942322884