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

Prolamin polypeptides from rye, wheat, and barley were comparedwith respect to the nature of their disulphide bonds, the effectsof reduction, and their molecular weights. Most secalins weredistinguished by their ease of reduction to polypeptides ofintermediate mobility, ranging in size from about 82–92kilodaltons (Kd), or to polypeptides with molecular weightsof 38 Kd that migrated 20–25% slower upon reduction. Athird group of secalin components had intermediate electrophoreticmobility on lactate gels, were unaffected by reducing agentsand had a molecular weight of 48 Kd. Wheat gliadin fractionscontained two types of component: the w-gliadins that couldnot be reduced further and the -, ß-, or -gliadinswhich were reduced to polypeptides of slightly lower electrophoreticmobilities than their native precursors. The predominant molecularweight range of gliadin polypeptides was 33–37 Kd. Thepredominant polypeptide components of hordein were nonreducible,with apparent molecular weights in the range from 50–60Kd. Few secalin or hordein polypeptides were similar in bothsize and reactivity to the gliadins. Key words: Secalin, Hordein, Gliadin, Molecular weight, Disulphide bond