Abstract
Further investigations of the fractionation of hordein by gel chromatography on Sephadex G-200 are described. The hordein fractions obtained by gel chromatography and those by continuous carrier-free electrophoresis were also characterized by means of continuous electrophoresis (or, respectively, gel chromatography), disc electrophoresis, amino acid analysis and molecular weight determination. The presence of six electrophoretically different fractions of hordein was firmly established. It was demonstrated that of the six hordein fractions only Fraction B has the property to yield reversibly aggregated molecules in urea medium. The remaining fractions are stable and behave as individual proteins. The correlation of the fractions obtained by the three methods employed is discussed. Further arguments for the necessity of a new classification of plant proteins based on their chemical and electrical properties rather than on their solubilities are presented.
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