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Reversible two-step unfolding of heme–human serum albumin: a1H-NMR relaxometric and circular dichroism study

✍ Scribed by Gabriella Fanali; Giampiero De Sanctis; Magda Gioia; Massimo Coletta; Paolo Ascenzi; Mauro Fasano


Publisher
John Wiley and Sons
Year
2008
Tongue
English
Weight
354 KB
Volume
14
Category
Article
ISSN
1432-1327

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The reversible binding of ethacrynic acid was characterized by a difference circular dichroism method. A 2/1 stoichiometry was determined for the [drug]/[HSA] (human serum albumin) complex. The reversible binding of ethacrynic acid to HSA determines direct competition with ligands that selectivity b