Thermodynamic parameters for 3-state thermal denaturation of human and bovine α-lactalbumin
✍ Scribed by Richard K.Owusu Apenten
- Publisher
- Elsevier Science
- Year
- 1995
- Tongue
- English
- Weight
- 494 KB
- Volume
- 262
- Category
- Article
- ISSN
- 0040-6031
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
## 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