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A third β‐Gliadin from Cappelle‐Desprez wheat
Author(s) -
Ewart John A. D.
Publication year - 1981
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.2740321211
Subject(s) - gliadin , chemistry , food science , gluten , amino acid , composition (language) , starch , carbohydrate , attraction , wheat starch , biochemistry , linguistics , philosophy
A third β‐gliadin has been isolated from Cappelle‐Desprez wheat. It is the middle member of a triplet of almost equally spaced bands that appears on starch‐gel electro‐phoresis. Surprisingly, it has no very close affinity with the fastest of these three bands. Although conforming to the amino acid composition expected in gliadins, the content of (His + Arg) is four less than in the fastest component, but the small molecular weight of only 27 000 compensates for this, so that the mobility at acid pH is only a little less than that of its faster companion. The protein appears to be single‐chain and free from SH groups and carbohydrate. Of the (Glx+Asx) content, 96% is amidated. Published analyses of β‐gliadins have been calculated to the same basis and compared.