Determination of the binding characteristics of dicoumarol to bovine serum abumin by UV/visible spectroscopic method
Date
2020
Journal Title
Journal ISSN
Volume Title
Publisher
U. P.
Abstract
8-Anilinonaphthalene-1-Sulfonic acid (ANS) was used as a probe to study the binding characteristics of Dicoumarol to Bovine Serum Albumin (BSA). The absorbance of ANS-BSA complex was decreased by the binding of Dicoumarol. This suggests that there is competition between Dicoumarol and ANS for the binding sites in the BSA. It means that ANS and Dicoumarol shared some of the binding sites on BSA. From the scatchard plot for the binding of Dicoumarol to BSA it is seen that Dicoumarol has three high affinity binding sites with association constants Kl=14.5245 x 106,10.6281x106,11.6811x106 respectively, and three secondary binding sites with association constants Kl =14.0084 x 10615.8816 x 106 and 19.2058x106 respectively and numerous low affinity binding sites.
Description
This research was conducted in collaboration with a of staff in the Department of Chemistry
Keywords
Binding characteristics, 8-anilinonaphthalene-1-sulfonic acid, dicoumarol, bovine serum albumin, scatchard plots, Department of Science Technology
Citation
Okoro, O. A., Onwumere, F. C., Enebeaku, C. K. & Akalezi, C. O. (2020). Determination of the binding characteristics of dicoumarol to bovine serum abumin by UV/visible spectroscopic method. World Journal of Engineering Research and Technology, 6(2), 94 - 107