A third β‐Gliadin from Cappelle‐Desprez wheat

Abstract

A third 8-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 electrophoresis. 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 OOO 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 singlechain and free from SH groups and carbohydrate. Of the (GlxSAsx) content, 96% is amidated. Published analyses of 8-gliadins have been calculated to the same basis and compared.

Isolation and partial characterisation of two low molecular weight durum wheat (Triticum durum) glutenins

“…Differences between the apparent molecular masses of DSG proteins were also observed by using SDS-PAGE either with or without previous reduction of the proteins (Kobrehel et a1 1988). A similar observation was reported for an isolated 8-gliadin (Ewart 1981). Conformational changes of these proteins, due to the different conditions, may be one of the explanations for all these discrepancies.…”