A three-state heat-denaturation of bovine α-lactalbumin
✍ Scribed by Richard K.Owusu Apenten
- Publisher
- Elsevier Science
- Year
- 1995
- Tongue
- English
- Weight
- 352 KB
- Volume
- 52
- Category
- Article
- ISSN
- 0308-8146
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📜 SIMILAR VOLUMES
By using both wide-angle neutron and small-angle X-ray scattering techniques, we have studied the denaturation processes of hen egg-white lysozyme (HEWL) and bovine a-lactalbumin (BLA) in dimethyl sulfoxide (DMSO)/water mixtures. Although these proteins are known to be highly homologous, the present
## Abstract The thermal denaturation of α‐lactalbumin was studied at pH 7.0 and 9.0 in aqueous 1,1,1,3,3,3‐hexafluoroisopropanol (HFIP) by high‐sensitivity differential scanning calorimetry. The conformation of the protein was analyzed by a combination of fluorescence and circular dichroism measure
## Abstract A first detailed comparison of the ^13^C spectra at high field of two lysozymes (human and egg‐white) and two α‐lactalbumins (human and bovine milk) is presented. Assignments were made on most of the resonance peaks in the aliphatic and aromatic regions of the denatured proteins. The re