STUDY OF THE INTERACTION OF BOVINE SERUM ALBUMIN WITH POTASSIUM SALTS: SPECTROSCOPIC APPROACH

S. BAKKIALAKSHMI*, B. SHANTHI**, V. PREMA***

*Department of Physics, Annamalai University, Annamalainagar – 608 002
**Centralized Instrumentation and Services Laboratory (CISL)
***Department of Physics, Annamalai University, Annamalainagar – 608 002

Abstract. By the analysis of steady state fluorescence spectrum and fluorescence intensity it was observed that the potassium salts have a strong ability to quench the intrinsic fluorescence of BSA through a static quenching procedure. Molar extinction coefficient and the Stoke’s shift were determined based on fluorescence quenching and UV results. The interaction of BSA with Potassium salts were also confirmed by UV absorption spectra. Time-resolved fluorescence experimental results showed that the binding of BSA to potassium salts induced conformational changes in BSA. The X-ray diffraction patterns of the mixtures of BSA and potassium slats were referred to that of pure BSA. The patterns obtained for the mixtures were different that of pure BSA. SEM photographs also shows the changes by potassium salts in BSA.
Key words: BSA, potassium salts, fluorescence quenching

Corresponding author’s e-mail: bakkialakshmis@rocketmail.com

Full text: PDF