[Spatial orientation interaction mechanism of three component complex of protein--BSA/SDS/Azur a system].
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.
Cao
Wen-gen
WG
Pharmaceutic Biotechnology Key Laboratory, College of Life Science, Nanjing University, Nanjing 210093, China
Jiao
Qing-cai
QC
Liu
Qian
Q
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
D001399:Azure Stains; D012710:Serum Albumin, Bovine; D012967:Sodium Dodecyl Sulfate; C025818:Azure A