Author
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Bietz, Jerold |
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Submitted to: American Association of Cereal Chemists Meetings
Publication Type: Abstract Only Publication Acceptance Date: 10/12/1997 Publication Date: N/A Citation: N/A Interpretive Summary: Technical Abstract: The importance and complexity of cereal endosperm storage proteins demand powerful fractionation and characterization methods. Electrophoresis has long been a useful method but has been slow, labor-intensive, and difficult to quantify. The ability to separate proteins by capillary electrophoresis (CE) in fused silica columns has overcome these shortcomings and provided a powerful new analytical tool. Methods were first developed to separate wheat gliadins. Using optimized buffer, capillary, and instrumental conditions, high-resolution separations can be obtained in 10 min or less and related to variety, class, or quality. The method is automatic and results are easy to quantify. Comparable results can be obtained on different instruments and in different laboratories, although buffer composition and pH are critical. A recent comparison of CE to reversed-phase HPLC and to gel electrophoresis has indicated the complementary nature of the methods and shown that CE should be useful for selection during breeding and in genetic studies. Wheat's high-molecular weight, quality-related glutenin subunits, also separate well based on size by CE in capillaries containing a sieving matrix as they do in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Still other separations such as of maize zein proteins are rapidly being developed. These and other separation modes are rapidly making CE an indispensable analytical tool for cereal protein analysis. |
