## Abstract By a combination of carboxymethylcellulose ion‐exchange chromatography and gel‐filtration α, β and γ‐gliadin proteins have been isolated in quantities large enough to be suitable for clinical feeding and baking tests. A pure ω‐gliadin has been obtained by the use of ion‐exchange chromat
Large scale isolation of gliadin fractions
✍ Scribed by Louis Charbonnier; Jacques Mossé
- Publisher
- John Wiley and Sons
- Year
- 1980
- Tongue
- English
- Weight
- 720 KB
- Volume
- 31
- Category
- Article
- ISSN
- 0022-5142
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✦ Synopsis
Abstract
The ω,‐ γ‐, and α‐gliadin groups were isolated by chromatography of 10 g of crude gliadin on Sulfopropyl Sephadex C50, followed by chromatographies of the SPS‐C50 fractions on Sephadex G100. The alcohol‐soluble glutenins separated from the SPS‐C50 fractions containing the γ‐ and β‐gliadins had lower contents of Asx, Ala and Tyr but higher contents of Thr, Ser and Met than the gliadins. On the basis of weights of the isolated fractions, the proportions of ω‐, γ‐, β‐ and α‐gladin groups in Cappelle wheat were estimated to be about 15, 30, 30 and 25% of the total gliadin, respectively. This method of isolation of the four gliadin groups is suitable for all wheat varieties, especially for the isolation of α‐gliadin.
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