Purification of hordein polypeptides by column chromatography using volatile solvents [barley, prolamin, gel filtration, ion exchange chromatography, amino acid composition]
1979
Schmitt, J.M. (Carlsberg Lab., Copenhagen (Denmark). Dept. of Physiology)
Hordein polypeptides C2 and B1 have been purified using gel filtration and ion exchange chromatography in volatile solvents. They are different in amino acid composition, the B1-hordein containing lower amounts of glutamine/glutamic acid and proline. By digestion with carboxypeptidase Y the C-terminal sequence Gly-Val-COOH was deduced for the B1 polypeptide whereas no clear sequence could be established from the amino acids Ser, Val, Ile and Met which were released from the C1-hordein. This indicates possible heterogeneity of the C2 component.
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