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World Journal of Engineering Research and Technology

( An ISO 9001:2015 Certified International Journal )

An International Peer Reviewed Journal for Engineering Research and Technology

An Official Publication of Society for Advance Healthcare Research (Reg. No. : 01/01/01/31674/16)

ISSN 2454-695X

Impact Factor : 7.029

ICV : 79.45

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Abstract

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.

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 onBSA. 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.

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