STUDIES ON WHEAT PLANTS USING CARBON-14 COMPOUNDS: XVI. FRACTIONATION OF A PERFORMIC ACID OXIDIZED PROTEIN

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Abstract
Wheat gliadin-C14was separated into ammonia-soluble and alkali-soluble fractions. Oxidation of the ammonia-soluble fraction with performic acid rendered the material water soluble and quantitatively converted the cystine and cysteine residues to cysteic acid. Little, if any, peptide bond hydrolysis resulted from the oxidation step. Five "protein-like" fractions were isolated by chromatography of the oxidation mixture on N,N′-diethylaminoethylcellulose (DEAE-cellulose).The specific activities of glutamic acid, proline, and leucine were found to vary widely with the fraction from which they were isolated. The fractions isolated are therefore characteristic of protein components with different biosynthetic histories.