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Fractionation and amino acid analysis of the salt‐soluble protein fractions of normal and high‐lysine barleys
Author(s) -
Rhodes Anthony P.,
Gill Anthony A.
Publication year - 1980
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.2740310508
Subject(s) - lysine , globulin , albumin , fractionation , chromatography , chemistry , sodium , polyacrylamide gel electrophoresis , biochemistry , amino acid , biology , enzyme , organic chemistry , immunology
High‐lysine barleys derive their high lysine content, in part, from an increase in the salt‐soluble proteins. These proteins were extracted in 0.5m sodium chloride from milled grain of the genotypes Hiproly, Risø 1508, Risø 7, Bomi, Vada and Ark Royal. The extracts were subsequently separated into albumins and globulins by dialysis against distilled water, and were examined by sodium dodecyl sulphate‐polyacrylamide gel electrophoresis (SDS‐PAGE) and amino acid analysis. SDS‐PAGE revealed that the polypeptides of both fractions were highly heterogeneous with respect to molecular weight. There were marked differences in the polypeptide composition of the albumin fraction of the high‐lysine genotypes compared to the normals, but relatively smaller differences in the globulins which were generally higher in lysine and lower in glutamic acid than the albumins. The albumin fraction of Hiproly had a very high level of lysine compared to the other genotypes and surprisingly the globulin fraction of Risø 1508 had a low lysine content. The consequences of these findings are discussed in relation to strategies for breeding high‐lysine barleys.