Chromatographic characterization of gluten proteins
1995
Michalik, I. | Petovsky, P.
Glutein proteins were isolated by precipitation 2 mol per l NaCl from 0.01 mol per l acetic acid, pH 2.9, purified by gel chromatography on Sephadexes G-25 and G-100 and fractionated by medium pressure liquid chromatography on SE-cellulose to 13 chromatographic subfractions. The sources of variability of gluten protein subfractions were computed for two sets of data. Over three years (1980-1982), three varieties of wheat (Yubileyna, Danubia and Kiyanka), at four stages of maturity and under four variants of increasing mineral nutrition (N, P, K) were evaluated. The sources of variability of the subfractions 1-13 influence the amount of protein of the individual subfractions in sequence as follows: year, stage of maturity, variety and mineral nutrition. The mineral nutrition significantly influences subfractions containing predominantly alpha- and beta-gliadin components and nonsignificantly influences subfractions of omega- and gama-gliadin components
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