Dye-Binding Capacities of Eleven Electrophoretically Separated Serum Proteins

Starch-gel electrophoresis has been found to be a valuable tool for the investigation of cereal proteins. Eight wheat varieties have been compared using aluminium lactate buffer of low pH. Although the albumin and globulin patterns appear to be very similar, there are significant differences among the patterns arising from the gluten proteins. I t is thought that these differences may be sufficiently marked to give rise to variations in protein quality.Comparison of wheat with barley, maize, oats and rye shows that profound differences exist between the patterns. Most of the proteins of the four last-named cereals are less soluble. Bands lying in the mobility range corresponding t o wheat gluten arc less marked in rye, present only in small quantities in barley, and undetectable in maize atid oats. IntroductionIt is over fifty years since Osbornel showed that there are at least two proteins in gluten,

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Simple device for continuous diffusion destaining of polyacrylamide gels

Gathercole¹,

Klein²

1971

Analytical Biochemistry

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Dye-Binding Capacities of Eleven Electrophoretically Separated Serum Proteins

Cited by 13 publications

References 9 publications

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The Binding of Drugs by Plasma Proteins

Starch‐gel electrophoresis of cereal proteins

Simple device for continuous diffusion destaining of polyacrylamide gels

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