## Abstract The high‐molecular‐weight glutenin subunits (HMW‐GS) of wheat gluten in their native form are incorporated into an intermolecularly disulfide‐linked, polymeric system that gives rise to the elasticity of wheat flour doughs. These protein subunits range in molecular weight from about 70K
Determination of the number of cysteine residues in high molecular weight subunits of wheat glutenin
✍ Scribed by Dr. Marie-Hélène Morel; Joëlle Bonicel
- Publisher
- John Wiley and Sons
- Year
- 1996
- Tongue
- English
- Weight
- 391 KB
- Volume
- 17
- Category
- Article
- ISSN
- 0173-0835
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
This work describes a carbon and proton solid-state NMR study of the hydration of a high molecular weight wheat glutenin subunit, 1Dx5. The effect of the presence of disulfide bonds on the hydration behavior of the subunit is investigated by a comparison of the unalkylated and alkylated forms of the
Eleven Pakistani hard white spring wheat cultivars, along with one durum wheat and two hard white American-grown wheat cultivars, were evaluated for their high-molecular-weight (HMW) glutenin subunit composition via sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). The relations