AbstractThe strongest band in the electrophoretic pattern of Cappelle‐Desprez gliadin owes its intensity to the coincidence of two proteins. These have been isolated and characterised. They have a fairly similar amino acid composition, typical of the gliadin class, and appear to be single polypeptide chains, free of SH groups and carbohydrate. Their molecular weights are 38 000 and 44 000. The higher mobility at pH 8.9 of the lighter molecule is attributed to its smaller size though the possibility also exists of its having fewer COO‐ groups. The equal mobility at acid pH arises because the extra resistance encountered by the larger molecule is balanced by a higher positive charge due to histidine. The proteins appear to correspond to theγ2andγ3Ponca gliadins isolated at Peoria, and this supports the idea that gliadins of equal mobility from different varieties have very similar structures. A rapid way of calculating recovered protein is ment
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