Characterization of components of heat-treated serum albumin with bromcresol green.
The interactions of bromcresol green with various components isolated from heat treated bovine serum albumin at 65 degrees C and pH 9.0 were studied spectrophotometrically. The difference spectra of the dye induced by native albumin and component 1, which has the same electrophoretic mobility as native albumin, had a trough at 616 nm and peak at about 668 nm, whereas those induced by the denatured monomer (component 1'), denatured dimer (component 2) and denatured trimer (component 3) had a trough at 610 nm and peak at 655 nm. From these difference spectra, it was concluded that component 1 is a mixture of at least two components (native and modified native forms) and that components 1', 2 and 3, formed during the process of denaturation, have essentially the same conformation in the environment of the binding sites for bromcresol green. A possible mechanism for the heat denaturation of serum albumin is proposed.
D001665:Binding Sites; D001961:Bromcresol Green; D003408:Cresols; D006358:Hot Temperature; D011485:Protein Binding; D011487:Protein Conformation; D011489:Protein Denaturation; D012710:Serum Albumin, Bovine; D013053:Spectrophotometry
D003408:Cresols; D012710:Serum Albumin, Bovine; D001961:Bromcresol Green