The comparative analysis of binding of three molecular fluorescent probes (fluorescein, eosin, and erythrosin), belonging to one homologous family, to human serum albumin (HSA) is made by Raman spectroscopy method. The binding of all three probes to binding Center I of HSA is registered. The charact
Raman spectroscopy in investigations of mechanism of binding of human serum albumin to molecular probe fluorescein
โ Scribed by I.M. Vlasova; A.M. Saletsky
- Publisher
- John Wiley and Sons
- Year
- 2008
- Tongue
- English
- Weight
- 107 KB
- Volume
- 5
- Category
- Article
- ISSN
- 1612-2011
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โฆ Synopsis
The mechanism of binding of molecular probe fluorescein to molecules of human serum albumin was studied by the Raman spectroscopy method. The position of binding Center on human serum albumin molecule for fluorescein is determined. The amino acid residues of albumin molecule, participating in binding of fluorescein at different pH values of solution, are established. The conformation rearrangements of globules of human serum albumin, taking place at binding of fluorescein at different pH values of solution, are registered.
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## Abstract Mn(II) ion binds to human serum albumin (HSA) through one strong binding site (__K__~A~ = 7.9 ร 10^3^ M^โ1^) and several weaker binding sites. Through competition assays it has been shown that the strong binding site lies in a region which has been previously identified as the Cd(II)๏ฃฟ Z