Citation: Su Xinyi, Liu Min, Yuan Mengjuan, Han Jun. Study on Thermal Stability of Human Serum Albumin at Different pH Values and Its Structural Reversibility[J]. Chemistry, ;2016, 79(4): 344-348. shu

Study on Thermal Stability of Human Serum Albumin at Different pH Values and Its Structural Reversibility

Su Xinyi ¹ ,
Liu Min ² ,
Yuan Mengjuan ¹ ,
Han Jun ^2,,

1.
1. School of Pharmacy, Liaocheng University, Liaocheng 252000;
2.
2. Institute of BioPharmaceutical Research, Liaocheng University, Liaocheng 252000

Corresponding author: Han Jun,
Received Date: 4 September 2015
Available Online: 29 October 2015
Fund Project:

The tertiary structure of human serum albumin (HSA) and the structure-reversibility at different pH values had been studied by DSC, DLS and CD. The results indicated that HSA proves to be the most stable structure at pH 7.0,and the melting temperature (T_m) is 68.17±0.06℃. The tertiary structure of HSA is changed at different pH values and the T_m of HSA is very close to the T_m at pH 7.0 when pH is adjusted back to 7.0 from different pH values. The size of HSA is larger at other different pH values than that at pH 7.0 and it gets smaller when pH is adjusted back to 7.0. The influence of pH on the secondary structure of HSA is detected by CD. Although HSA can be refolded when adjusted back to 7.0 from different pH values, it can't return back to the structure of HSA at pH 7.0.
- DSC,
- Dynamic light scattering (DLS),
- Circular dichroism (CD),
- Partical size,
- Human serum albumin (HSA)
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