Electrophoresis of gliadins in long acrylamide gels: Method and nomenclature
✍ Scribed by Dr. Gérard Branlard; Brigitte Picard; Christian Courvoisier
- Publisher
- John Wiley and Sons
- Year
- 1990
- Tongue
- English
- Weight
- 622 KB
- Volume
- 11
- Category
- Article
- ISSN
- 0173-0835
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
Gliadins, defined as wheat kernel storage proteins soluble in 70% ethanol, possess an electrophoretic diversity permitting us to identify different varieties. Because of genetic proximity, however, it sometimes proves impossible to distinguish between different varieties using standard methods. An electrophoresis method, utilizing a discontinuous buffer system with aluminum lactate and potassium lactate in the gel and sodium lactate in the electrode vessels, is described for two types of gels 18 cm and 32 cm in length. The number of bands in higher than with standard methods, and is significantly increased with long gels, facilitating the distinction between varieties. A nomenclature for the new bands is presented for several widely different cultivars.
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Previous results have shown that the mobility of proteins and peptides in acrylamide-gel electrophoresis is strongly dependent on the concentration of the gel (1, 2). Generally, the more concentrated the gel, the lower is the mobility. In presenting our earlier results (2) for proteins of molecular
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