Abstract
Four sub-units of vicilin were separated by sodium dodecyl sulphate gel electrophoresis and their molecular weights determined by calibration. The amino acid composition of vicilin was determined by ion-exchange chromatography and by other methods for half-cystine and tryptophan. Tryptic peptide maps and N-terminal analysis following cyanogen bromide cleavage, were used to deduce a chemical molecular weight of vicilin of 100–130 × 10 3. These structural results on vicilin are discussed in relationship to its biological role.
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