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Relationship between wheat proteins
Author(s) -
Booth M. R.,
Ewart J. A. D.
Publication year - 1970
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740210406
Subject(s) - gliadin , globulin , storage protein , biology , amino acid , trypsin , albumin , biochemistry , trypsin inhibitor , protein tertiary structure , genetics , gluten , gene , enzyme , immunology
Recent evidence including amino acid analyses, immunological tests and fingerprinting suggests that the gliadins of wheat varieties have evolved from a common ancestral protein by a series of mutations. No evidence to support a relationship of this nature between the gliadin, albumin and globulin classes was found. Confirmation of the genetic link between wheat and barley is provided by the close structural affinity between purothionin and its barley counterpart. There are some similarities in amino acid composition between a barley trypsin inhibitor and a wheat albumin. Available evidence, though scanty, is significant enough to justify the generalisation that storage proteins of identical mobility in different wheat varieties have closely similar primary and tertiary structures. Although the individual gliadins within a given variety are mutationally linked, their tertiary structures as judged by immunological tests show characteristic differences.