The heterogeneity of the high-sulphur fraction of reduced and S-carbdxymethylated proteins from wool was studied by starch-gel electrophoresis in aqueous urea-acetic acid at pH 2.4. This system gives better resolution than previously used alkaline buffers. A typical preparation was found to give twe
โฆ LIBER โฆ
Helix-rich Fraction from the Low-sulphur Proteins of Wool
โ Scribed by CREWTHER, W. G.; HARRAP, B. S.
- Book ID
- 109644989
- Publisher
- Nature Publishing Group
- Year
- 1965
- Tongue
- English
- Weight
- 130 KB
- Volume
- 207
- Category
- Article
- ISSN
- 0028-0836
- DOI
- 10.1038/207295a0
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## Synopsis S-Carboxymethyl (SCM) kerateine preparations from a range of keratins were fractionated by acid precipitation into low-sulfur (SCMKA) and high-sulfur (SCMKB) fractions. Amino acid analyses and optical rotatory dispersion measurements on the SCMKA fractions from different keratins indic