Abstract
Different fractions of zeins, the alchohol soluble proteins of maize, were analyzed by non-ionic detergent acid urea-polyacrylamide gel electrophoresis (NDAU-PAGE) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (NDAU-PAGE) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). By using NDAU-PAGE, the zein-1 fraction can be resolved at least in 7 polypeptide components, while only 3 protein bands can be observed by SDS-PAGE. Zein-2 showed at least 2 additional components as compared with zein-1 when analyzed by SDS-PAGE and a total of 10 bands in the presence of non-ionic detergent, acetic acid and urea. Combining both techniques in a two-dimensional arrangement, 16 components can be resolved for zein-1 proteins. This method has been used here to distinguish the protein patterns of a normal variety and one containing the opaque-2 (o2) mutation.
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