Abstract
Quantitative extraction of salt and water soluble proteins from Hiproly, CI 4362 and Bomi barley was performed and their content of the lysine rich SP II albumin determined by a single radial immunodiffusion assay. The elevated content of SP II albumin in Hiproly accounted for 37% of the difference in crude protein lysine between Hiproly and Bomi and for 19% between Hiproly and its low lysine sisterline CI 4362. Apart from the lysine rich SP II albumin, other proteins contribute to the high lysine content of Hiproly.
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