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Cereal Chem 68:512-515   |  VIEW ARTICLE

Electrophoretic Study of Some High Molecular Weight Proteins of the Acetic Acid-Insoluble Residue of Wheat Flours.

D. Sievert, H. D. Sapirstein, and W. Bushuk. Copyright 1991 by the American Association of Cereal Chemists, Inc. 

Acetic acid-insoluble (residue) protein fractions of flours of seven wheat varieties were studied by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Electrophoretic patterns of unreduced SDS-buffer extracts from flour residue fractions revealed a group of relatively high molecular weight (HMW) proteins having similar electrophoretic characteristics. The HMW proteins of one variety (Neepawa) were characterized further by two-dimensional SDS-PAGE under nonreducing and reducing conditions. The two-dimensional separation showed that the HMW proteins comprised several subunits. Three of these proteins, designated B-2, B-3, and B-4, share some correspondence with the triplet band proteins and appear to be partly composed of four large subunits resolved in pairs with molecular weights of about 56 and 52 kilodaltons.

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