The interaction of bovine serum albumin (BSA), sodium dodecyl sulphate (SDS) and Azur A(AA) was studied by spectral probe. The influence of the molar ratio of SDS/BSA on the absorption spectra of BSA-SDS-AA complex was investigated. It was found that the new absorption peak and color changes generated by BSA-SDS-AA complex arose from the difference in the spatial orientation aggregative degree of AA binding on BSA-SDS-AA complex.
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