title: Temperature-induced conformational transition of bovine serum albumin in neutral aqueous solution by reversed-phase liquid chromatography.
abstract: The temperature-induced conformational transition of bovine serum albumin (BSA) in neutral aqueous solution was studied using intrinsic fluorescence emission spectrum, reversed-phase liquid chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and the conformation transition thermodynamic parameters were determined in the temperature range 12-50 °C. The results showed that, in the temperature range 12-20 °C, BSA only existed in a single conformation state A, while in the temperature range 22-50 °C, it existed in two different conformation states: A and B. The percentage of conformation state A decreased while that of conformation state B increased with the increase in temperatures, and when temperature approached 50 °C conformation state B accounted for approximately 25% of all conformation states of BSA. In the conformational transition of BSA from conformation state A to conformation state B, the positive enthalpy change, entropy change and free energy changes demonstrated that the conformational transition was endothermic, nonspontaneous and mainly entropy-driven.
authors.affiliation: College of Life Science, Northwest University, Xi'an, 710069, China.
authors.forename: Liujiao
authors.initials: L
authors.lastname: Bian
authors.forename: Dan
authors.initials: D
authors.lastname: Wu
authors.forename: Wei
authors.initials: W
authors.lastname: Hu
mesh_terms: D000818:Animals; D002417:Cattle; D056148:Chromatography, Reverse-Phase / Q000379:methods*; D004591:Electrophoresis, Polyacrylamide Gel; D011487:Protein Conformation; D012710:Serum Albumin, Bovine / Q000737:chemistry* / Q000378:metabolism; D013816:Thermodynamics; D014867:Water
chemical_list: D014867:Water; D012710:Serum Albumin, Bovine
keywords: bovine serum albumin; conformational transition; reversed-phase liquid chromatography; thermodynamic parameters