Characterization of high molecular weight gliadin and low-molecular-weight glutenin subunits of wheat endosperm by two-dimensional electrophoresis and the chromosomal location of their controlling genes
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Gliadins, here defined as those proteins of defatted wheat endosperm which dissolve in 70% (v/v) ethanol at room temperature, were fractionated by gel filtration using Sephadex G-100. The protein which eluted with the void volume of the column, often described as high-molecular-weight (HMW) gliadin, was fractionated by the two different, two dimensional gel electrophoresis procedures of O'Farrell (1975) and O'Farrell et al. (1977). The next two fractions to elute from the gel column, ω-gliadin and α-, β-, γ-gliadin, were analysed similarly. The subunits of HMW gliadin and the classical (i.e. non-aggregated) gliadins map at distinctive positions on the
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