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Cereal Chem. 71:122-129   |  VIEW ARTICLE

Adsorption Chromatography on Controlled-Pore Glass Beads of Acetic- Acid-Soluble Wheat Gluten Proteins.

A. D. B. Peruffo, A. Curioni, G. Pressi, N. E. Pogna, and A. Zamorani. Copyright 1994 by the American Association of Cereal Chemists, Inc. 

Adsorption chromatography on 2,000-Angstrom controlled-pore glass beads, performed by frontal analysis in the absence of any detergent or chaotropic agent, was found to be capable of highly reproducible separation of the acetic-acid-soluble unreduced proteins from wheat gluten. Glutenin polymers with molecular mass greater than 10(7) Da and free from both starch and monomeric proteins were recovered. Furthermore, a number of polymers with lower molecular mass differing in subunit composition were obtained. The polymers retained their ability to make up the gluten. Gluten proteins were adsorbed on the glass beads with a sequential and competitive mechanism involving hydrophobic interactions. Proteins desorbed by increasing urea concentration in the eluent up to 6M were found to be gamma-gliadins encoded by the group 1 chromosomes, along with glutenin polymers.

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