Interaction of Bovine Serum Albumin and Hexadecyl Pyridinium Bromide Study by Surfactant Selective Electrode and Spectrophotometry
Surfactant selective electrode and spectrophotometric were used to study the effect of hexadecyl pyridinium bromide (HPB) on the conformation changes of bovine serum albumin (BSA) in aqueous solution. Our previous finding suggested multi-state serum albumin BSA. EMF plots — versus logarithm of HPB concentration revealed also four breaks. The saturated quantities of the HPB binding were 33,93,155,255 mol/mol. The Reynolds and Hill equations were applied to obtain co-operative HPB bindings to BSA. Gibbs free energy was calculated from binding data. Spectrophotometry study suggests hydrophobic interaction of HPB with BSA.
KeywordsBovine Serum Albumin Surfactant Concentration Micro Calorimetry Hill Equation Binding Isotherm
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- 3.Wasylewski, Z. (1979) Acta Biochemica Polonica Vol. 26: No. 3: 195–203.Google Scholar
- 4.Ancell, H. (1939) Lancet 1: 222–231.Google Scholar
- 8.Davidson, C.J. Ph.D. thesis (University of Aberdeen, 1983 ).Google Scholar
- 10.Painter, D.M. Ph.D. Thesis (University of Salford, 1988 ).Google Scholar
- 11.Steinhardt, J., and Reynolds, J.A. (1968) Multiple Equilibiria in Protein, pp. 239–302, Academic press, New York.Google Scholar
- 17.Hill, A.V. (1910) J. Phsio.Google Scholar
- 18.Strop, (1987) Chem. Commun. 52 (5): 1362–1374.Google Scholar