[Some new results from isolation and fractionation of low molecular weight wheat proteins].

The alcohol-soluble wheat gluten fraction (gliadine) and the petroleum-ether-soluble wheat protein fraction (purothionine) were isolated and analysed. The gliadine fraction was itself fractionated by gel chromatography (Sephadex G-100). The partial hydrolysis of sub-fractions (molecular weight 20000-30000) yielded (after separation by gel and ion-exchange chromatography) several peptide fractions. The amino-acid composition and the N- and C-terminal groups of the gliadine fractions were determined. Characteristic differences were stated between various fractions. By means of gel chromatography, purothionine was separated into 4-6 fractions. The study of the amino-acid composition and of the N-terminal groups of the fractions revealed differences in both properties.