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Cereal Chem 56:513 - 516.  |  VIEW ARTICLE
Studies of Glutenin. XIV. Gel Filtration and Sodium Dodecyl Sulfate Electrophoresis of Glutenin Solubilized in Sodium Stearate.

Z. Hamauzu, K. Khan, and W. Bushuk. Copyright 1979 by the American Association of Cereal Chemists, Inc. 

Glutenin was dissolved in sodium stearate-water solvent and subjected to gel-filtration chromatography on Sephadex G-150 and G-200, using tris-hydrochloric acid-sodium dodecyl sulfate (SDS) buffer, and on Bio- gel P-300, using tris-borate-SDS buffer as eluants. One major fraction (peak I), eluting in the void volume, and two minor fractions (peaks II and III) were obtained. SDS-polyacrylamide gel electrophoresis (PAGE) showed that the reduced proteins of peak I contained the total subunit pattern of glutenin, with subunit molecular weights ranging from 12,000 to 134,000. Peak II, contained predominantly the 35,000 and 45,000 subunits, and peak III was predominantly the 12,000 subunit. Gel-filtration and SDS-PAGE results also showed that the disulfide bonds of glutenin are not cleaved by sodium stearate.

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