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摘要
Thermal conformational changes of human serum albumin (HSA) and bovine serum albumin (BSA) in different buffer solutions, in the pH range 3.0 - 9.0, are investigated by fluorescence spectroscopy. Temperature increasing in the range 25 - 90 degrees C induces partially reversible changes in the 3D structure of the two serum albumins. At pH = 3.0 (albumin form E) and pH = 8.0 (B form) the renaturation degree is greater than that manifested at pH = 4.0 (F form) and pH = 7.0 (N form). Instead, at pH = 5.0 and pH = 6.0, both serum albumins present states, whose thermal denatured conformations cannot be renatured by a stepwise temperature decrease.
- 出版日期2011-6
