Comparative analysis of refolding of chemically denatured β-lactoglobulin types A and B using the dilution additive mode
| Autor: | Ali Akbar Saboury, Adeleh Divsalar, H. Mansoori-Torshizi, A.A. Moosavi-Movahedi |
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| Rok vydání: | 2006 |
| Předmět: |
Protein Folding
Protein Renaturation Lactoglobulins In Vitro Techniques Biochemistry Protein Structure Secondary chemistry.chemical_compound Drug Stability Structural Biology Animals Sorbitol Thermal stability Sugar Molecular Biology chemistry.chemical_classification Aqueous solution Chromatography Circular Dichroism beta-Cyclodextrins General Medicine Fluorescence Amino acid Dilution Kinetics Glucose Spectrometry Fluorescence chemistry Yield (chemistry) Thermodynamics Cattle |
| Zdroj: | International Journal of Biological Macromolecules. 38:9-17 |
| ISSN: | 0141-8130 |
| DOI: | 10.1016/j.ijbiomac.2005.12.010 |
| Popis: | The kinetic refolding of beta-lactoglobulin (BLG), types A and B, by beta-cyclodextrin, glucose and sorbitol has been investigated in aqueous solution using fluorescence, far UV-CD and UV-spectrophotometric techniques. A new Pd-complex has been used to denature the protein. CD and fluorescence studies indicated that when incubated with sugar, the denatured BLG is refolded into the native-like structure through the dilution additive mode resulting in a higher yield of active protein than without sugar. CD studies show that these sugars can induce a non-native alpha-helical structure in denatured BLG-A and -B, then aid in the refolding of the protein. Based on the present study, these sugars have a different effect on BLG-A than BLG-B because of their differences in protein thermal stability. BLG-A has a higher thermal stability than BLG-B due to differences in the amino acid sequences. |
| Databáze: | OpenAIRE |
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