Hydration Properties of the Molecular Chaperone α-Crystallin in the Bovine Lens
✍ Scribed by M. A. Babizhayev; G. M. Nikolayev; S. N. Goryachev; J. Bours; R. Martin
- Book ID
- 111560220
- Publisher
- Springer
- Year
- 2003
- Tongue
- English
- Weight
- 335 KB
- Volume
- 68
- Category
- Article
- ISSN
- 0006-2979
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Recently we reported on the separation of the subunits of the bovine eye lens protein a-crystallin by means of fast protein liquid ehromatography-chromatofocusing in concentrated ureal. We noted that the pH at which the CYAN and aAz subunits eluted from the column differed by 0.41 pH unit from their
## Abstract A combination of mass spectrometric techniques has been used to investigate the amino acid sequence and post‐translational modifications of αB‐crystallin isolated from bovine lenses by gel filtration chromatography and reversed‐phase high performance liquid chromatography. Chromatograph