## Abstract The interaction of Ce^3+^ to bovine serum albumin (BSA) has been investigated mainly by fluorescence spectra, UV–vis absorption spectra, and circular dichroism (CD) under simulative physiological conditions. Fluorescence data revealed that the quenching mechanism of BSA by Ce^3+^ was a
Spectrofluorimetric study of the binding of 1-anilinonaphthalene-8-sulfonate to bovine serum albumin
✍ Scribed by A. Suárez Varela; M. I. Sández Macho; J. Miñones
- Publisher
- John Wiley and Sons
- Year
- 1992
- Tongue
- English
- Weight
- 339 KB
- Volume
- 81
- Category
- Article
- ISSN
- 0022-3549
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
Protein surface hydrophobicity can be measured by the Ñuorescent probe method. The e †ect of heat treatment on Brassica napus (rapeseed) albumin (napin) interactions with a Ñuorescent probe, anilinonaphthalene-8-sulphonic acid (ANS) was investigated by Ñuorescent titration. Upon heating to 100¡C for
The kinetics of the binding of librium to bovine serum albumin w2re investigated at an ionic strength of 0.15 M, in the pH-range between 5.5 and 10.5. using the temperature-jump method. TWO relaxation times were observed. The first. rapid one is assigned to the equilibrium between reactants and comp