Isolation and characterization of gliadin-like subunits from glutenin
1973
Bietz, J.A. | Wall, J.S.
The polypeptide subunits of wheat glutenin obtained after reductive cleavage of disulphide bonds have been separated into 2 fractions by a modified Osborne technique. Approx. 62% of the subunits by wt. are soluble, as is gliadin, in neutral 70% ethanol; the ethanol-soluble subunits are mainly of 44 000 mol. wt. (MW). The ethanol-insoluble glutenin subunit fraction is markedly different in amino acid composition, and consists of high-MW subunits, and some of lower MW. Sodium dodecyl sulphate electrophoresis, starch-gel electrophoresis, and amino acid analyses suggested that some ethanol-soluble subunits of reduced glutenin may be equivalent to subunits of high-MW gliadin. To test this possibility, both fractions were reduced and alkylated and 44 000-MW subunits were isolated and partially characterized.
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