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.
The single radial immunodiffusion assay for quantitative determination of SP II albumin permits the separation of high-lysine from low-lysine lines in progenies from crosses with Hiproly. Identification of plants carrying the Hiproly gene can be carried out by single seed analysis and is more reliable than identification by β-amylase content or by dye-binding capacity measurements. Degree of grain hardness as measured by energy required for milling can vary independently of the content of SP II albumin.
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Jonassen, I. Characteristics of hiproly barley II. Quantification of two proteins contributing to its high lysine content. Carlsberg Res. Commun. 45, 59–68 (1980). https://doi.org/10.1007/BF02906532
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DOI: https://doi.org/10.1007/BF02906532