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Cereal Chem 64:380-384   |  VIEW ARTICLE

High-Resolution Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis of Soybean (Glycine max L.) Seed Proteins.

S. K. Sathe, G. G. Lilley, A. C. Mason, and C. M. Weaver. Copyright 1987 by the American Association of Cereal Chemists, Inc. 

Thirty-one soybean (Glycine max L.) varieties were electrophoretically evaluated using two high-resolution sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis (PAGE) procedures. Increased tris (tris[hydroxymethyl]aminomethane) concentration in the separating gel (8-25% linear acrylamide gradient) and the running buffer afforded high resolution of soybean-protein subunits comparable to that of the urea SDS-PAGE system. When compared with urea SDS-PAGE, non-urea SDS-PAGE permitted the following: better resolution of polypeptides in the molecular weight range of 29,000 to 32,000; differentiation of genetically closely matched pairs (Century and Century 84; Wells II and Miami); identification of a unique doublet of polypeptides in the Raiden variety; and in some varieties, identification of a peptide with higher mobility than that of the A5 subunit of the 11S globulin.

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