Cereal Chem 56:468 - 473.  |  VIEW ARTICLE
Amino Acid Composition of Total Protein and Electrophoretic Behavior of Protein Fractions of Barley.

A. M. El-Negoumy, C. W. Newman, and B. R. Moss. Copyright 1979 by the American Association of Cereal Chemists, Inc. 

Total protein from 23 barley cultivars of various origins, grown at the Montana Agricultural Experiment Station, was separated into albumin-globulin, hordein, and glutelin fractions. The protein fractions were examined by sodium dodecyl sulfate disc gel electrophoresis. From 13.0 to 19.6 total protein occurred in the barleys, of which 27.5 to 39.8% were albumin-globulin, 17.2 to 36.9% were hordein, and 23.6 to 41% were glutelin. The total protein of most barleys had essentially the same amino acid composition except Hiproly, which had much higher lysine, but low levels of alanine, arginine, glutamic acid, and cystine/2. The albumin-globulin contained 12 components occurring in six types of electrophoretic combinations. Three of the major components occurred at varying concentrations in all six types of electrophoretic patterns and in all 23 barley cultivars. Hordeins contained seven components at various levels of concentration in five different electrophoretic combinations. Fifteen different gluetlin components were found in four types of electrophoretic combinations. Only one of these components, which had the lowest molecular weight (12,400), occurred in three of the four combinations.