title: Comparative analysis of refolding of chemically denatured beta-lactoglobulin types A and B using the dilution additive mode.
abstract: 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.
authors.affiliation: Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran.
authors.forename: A
authors.initials: A
authors.lastname: Divsalar
authors.forename: A A
authors.initials: AA
authors.lastname: Saboury
authors.forename: A A
authors.initials: AA
authors.lastname: Moosavi-Movahedi
authors.forename: H
authors.initials: H
authors.lastname: Mansoori-Torshizi
mesh_terms: D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D004355:Drug Stability; D005947:Glucose / Q000494:pharmacology; D066298:In Vitro Techniques; D007700:Kinetics; D007782:Lactoglobulins / Q000737:chemistry*; D017510:Protein Folding; D020673:Protein Renaturation / Q000187:drug effects; D017433:Protein Structure, Secondary; D013012:Sorbitol / Q000494:pharmacology; D013050:Spectrometry, Fluorescence; D013816:Thermodynamics; D047392:beta-Cyclodextrins / Q000494:pharmacology
chemical_list: D007782:Lactoglobulins; D047392:beta-Cyclodextrins; D013012:Sorbitol; D005947:Glucose; C031215:betadex