Dialysis and circular dichroism study of the binding of sulfaethidole to crystalline and fraction V bovine serum albumin
β Scribed by H. B. Kostenbauder; M. J. Jawad; J. H. Perrin; V. Averhart
- Publisher
- John Wiley and Sons
- Year
- 1971
- Tongue
- English
- Weight
- 302 KB
- Volume
- 60
- Category
- Article
- ISSN
- 0022-3549
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
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
## Abstract The interaction of Ce^3+^ to bovine serum albumin (BSA) has been investigated mainly by fluorescence spectra, UVβvis absorption spectra, and circular dichroism (CD) under simulative physiological conditions. Fluorescence data revealed that the quenching mechanism of BSA by Ce^3+^ was a
The binding of cupric ions to bovine serum albumin was investigated by using a cupric-ion-specific electrode. When using a modified form of the Scatchard equation, it was determined that there are at least two classes of binding sites on bovine serum albumin for cupric ions. One class has three bind