Comparison of DMSO-induced denaturation of hen egg-white lysozyme and bovine α-lactalbumin
✍ Scribed by H Iwase; M Hirai; S Arai; S Mitsuya; S Shimizu; T Otomo; M Furusaka
- Publisher
- Elsevier Science
- Year
- 1999
- Tongue
- English
- Weight
- 117 KB
- Volume
- 60
- Category
- Article
- ISSN
- 0022-3697
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✦ Synopsis
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 results indicate that the structure of BLA is liable to be destroyed by the addition of DMSO in comparison with the case of HEWL. DMSO-induced denaturation is suggested to relate to the collapse of hydration shell surrounding the protein surface.
📜 SIMILAR VOLUMES
Vibrational Raman optical activity (ROA) spectra of the calcium-binding lysozyme from equine milk in native and nonnative states are measured and compared with those of the homologous proteins hen egg white lysozyme and bovine ␣-lactalbumin. The ROA spectrum of holo equine lysozyme at pH 4.6 and 22°
## 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