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DETERMINATION OF THE BINDING CHARACTERISTICS OF DICOUMAROL TO BOVINE SERUM ALBUMIN BY UV /VISIBLE SPECTROSCOPIC METHOD
Okoro O. A.*, Onwumere F. C., Enebeaku C. K. and Akalezi C. O.
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 106 15.8816 x 106 and 19.2058x106 respectively and numerous low affinity binding sites.