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°
Comparison of the binding of Ca2+ and Mn2+ to bovine α-lactalbumin and equine lysozyme
✍ Scribed by Johan Desmet; Herman Van Dael; Frans Van Cauwelaert; Katsutoshi Nitta; Shintaro Sugai
- Publisher
- Elsevier Science
- Year
- 1989
- Tongue
- English
- Weight
- 412 KB
- Volume
- 37
- Category
- Article
- ISSN
- 0162-0134
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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 metal ion requirement of myosin‐ADP binding was investigated by use of Mn^2+^. Mn^2+^ binds to two sets of noninteracting sites on myosin which are characterized by affinity constants of 10^6^ and 10^3^, M^−1^ at 0.016 M KCl concentration. The maximum number of sites is 2 for the hi