Abstract
The conformation of bovine serum fetuin (BSF) was examined over the pH 7.0-12.9 regions by circular dichro-ism, intrinsic fluorescence and ANS binding. We observed that at higher pH, BSF exists in alkaline unfolded state. Our results provided evidence that correlates simultaneous formation of secondary structure followed by accumulation of hy-drophobic clusters.
Original language | English |
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Pages (from-to) | 660-666 |
Number of pages | 7 |
Journal | Protein and Peptide Letters |
Volume | 17 |
Issue number | 5 |
DOIs | |
Publication status | Published - 2010 |
Externally published | Yes |
Keywords
- Acetonitrile
- Alkali denaturation
- Bovine serum fetuin
- Circular dichroism
- Trifluoroethanol