Journal
JOURNAL OF SOLUTION CHEMISTRY
Volume 38, Issue 8, Pages 1071-1077Publisher
SPRINGER/PLENUM PUBLISHERS
DOI: 10.1007/s10953-009-9430-3
Keywords
Bovine serum albumin; Interaction; Puerarin; Temperature; Ion
Categories
Funding
- Natural Science Foundation of Nantong University [07z026]
Ask authors/readers for more resources
The effects of temperature and common ions on binding of puerarin to bovine serum albumin (BSA) are investigated. The binding constants (K (a)) between puerarin and BSA are 1.13x10(4) La <...mol(-1) (20 A degrees C) and 1.54x10(4) La <...mol(-1) (30 A degrees C), and the number of binding sites (n) is (0.95 +/- 0.02). However, at a higher temperature (40 A degrees C) the stability of the puerarin-BSA system decreases, which results in a lower binding constant (1.58x10(3) La <...mol(-1)) and number of binding sites (n=0.73) of the puerarin-BSA system. However, the presence of Cu2+ and Fe3+ ions increases the binding constants and the number of binding sites in the puerarin-BSA complex.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available