The amino acid content of the proteins of barley grains

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Abstract
Preparations are described of the 4 chief protein fractions of barley grains, i.e. albumin, globulin, prolamin (horedein) and glutelin (hordenin). One of these, hordenin, is prepared by a new method involving iso-electric reprecipitation from solutions of different ethanol content. Amino acid analyses of the various preparations were compared with those for the protoplasmic protein of barley seedlings. While the albumin and globulin closely resemble the protoplasmic proteins, hordein and hordenin are far richer in amide, glutamic acid and proline, these accounting for over 60% of the hordein N. In germination, presumably, the deficiency in aspartic acid, alanine, glycine, lysine, arginine, isoleucine, tryptophan and threonine must be made good from glutamine and proline residues of the storage proteins.