Bromophenol blue binding as a probe to study urea and guanidine hydrochloride denaturation of bovine serum albumin.
作者： A. A. Abd. Halim , H. A. Kadir , S. Tayyab
DOI: 10.1093/JB/MVN036
关键词: Bromophenol blue 、 Denaturation (biochemistry) 、 Absorption (chemistry) 、 Bovine serum albumin 、 Hydrochloride 、 Wavelength range 、 Guanidine 、 Chromatography 、 Urea 、 Chemistry
摘要: Urea and guanidine hydrochloride (GdnHCl) denaturation of bovine serum albumin (BSA) were investigated using bromophenol blue (BPB) binding as a probe. Addition BPB to BSA produced an absorption difference spectrum in the wavelength range, 525-675 nm with minimum at 587 maximum 619 nm. The magnitude (DeltaAbs.) decreased on increasing urea/GdnHCl concentration followed curve. was found be two-state, single-step transition. transitions started 1.75 0.875 M completed 6.5 3.25 mid point occurring around 4.0 1.5 urea GdnHCl concentrations, respectively. value free energy stabilization, DeltaGDH2O determined from curves 4041 4602 cal/mol, Taken together, these results suggest that can used probe study BSA.
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