title: [Spatial orientation interaction mechanism of three component complex of protein--BSA/SDS/Azur a system].
abstract: 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.
authors.affiliation: Pharmaceutic Biotechnology Key Laboratory, College of Life Science, Nanjing University, Nanjing 210093, China
authors.forename: Wen-gen
authors.initials: WG
authors.lastname: Cao
authors.forename: Qing-cai
authors.initials: QC
authors.lastname: Jiao
authors.forename: Qian
authors.initials: Q
authors.lastname: Liu
mesh_terms: D000818:Animals; D001399:Azure Stains / Q000737:chemistry* / Q000378:metabolism; D002417:Cattle; D015394:Molecular Structure; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000737:chemistry* / Q000378:metabolism; D012967:Sodium Dodecyl Sulfate / Q000737:chemistry* / Q000378:metabolism; D013053:Spectrophotometry
chemical_list: D001399:Azure Stains; D012710:Serum Albumin, Bovine; D012967:Sodium Dodecyl Sulfate; C025818:Azure A