A Comparative Study of Disulphide-Bonding and Molecular Weights of Purified Fractions from Secalin, Gliadin, and Hordein

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Abstract
Prolamin polypeptides from rye, wheat, and barley were compared with respect to the nature of their disulphide bonds, the effects of reduction, and their molecular weights. Most secalins were distinguished by their ease of reduction to polypeptides of intermediate mobility, ranging in size from about 82–92 kilodaltons (Kd), or to polypeptides with molecular weights of 38 Kd that migrated 20–25% slower upon reduction. A third group of secalin components had intermediate electrophoretic mobility on lactate gels, were unaffected by reducing agents and had a molecular weight of 48 Kd. Wheat gliadin fractions contained two types of component: the w-gliadins that could not be reduced further and the α-, β-, or γ-gliadins which were reduced to polypeptides of slightly lower electrophoretic mobilities than their native precursors. The predominant molecular weight range of gliadin polypeptides was 33–37 Kd. The predominant polypeptide components of hordein were nonreducible, with apparent molecular weights in the range from 50–60 Kd. Few secalin or hordein polypeptides were similar in both size and reactivity to the gliadins.

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