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Protein binding investigation by difference circular dichroism: Native and acetylated human serum albumins

✍ Scribed by Carlo Bertucci; Alessandro Viegi; Giorgio Ascoli; Piero Salvadori


Publisher
John Wiley and Sons
Year
1995
Tongue
English
Weight
500 KB
Volume
7
Category
Article
ISSN
0899-0042

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✦ Synopsis


A modified albumin was prepared by selective reaction of Lys,, with acetyl salicylic acid. Protein binding investigation was camed out on native and modified proteins by difference circular dichroism (ACD). Acetylation of Lyslgg reduces sigdicantly the effects of the interaction between drugs in the stereoselective HSA bindmg at specific binding areas.


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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