PREPARATION OF GLUTENIN IN UREA SOLUTIONS

Author:

Cook W. H.,Alsberg C. L.

Abstract

A new method has been developed for preparing glutenin, using concentrated urea solution as a dispersion medium. The starch is removed from the dispersion by passing it through a Sharpies supercentrifuge. The glutenin is then removed from the gliadin by precipitation: (a) by adding magnesium sulphate to about 0.17 of saturation; or (b) by adding water until the urea is diluted to about 10% concentration. Alcohol precipitation is unsatisfactory, since the glutenin loses much of its original solubility. Drying, even at room temperature, renders glutenin insoluble in 30% urea solution. Different samples of glutenin isolated by the urea method have similar amide and arginine nitrogen contents. The amount of these constituents is intermediate between the values reported for glutenin isolated from alkali, and that isolated from acid. While urea solutions denature some proteins, they affect glutenin less than dilute alkalies, as judged by the sulphydryl test, and no more than dilute acids. Neutral urea solutions permit a study of the physical properties of glutenin without previous exposure to extremes of hydrogen ion concentration. This method should be applicable to the isolation of glutenins from other seeds.

Publisher

Canadian Science Publishing

Subject

Pharmacology (medical),Complementary and alternative medicine,Pharmaceutical Science

Cited by 5 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

1. Chromatography of the Proteins from Wheat Flour soluble in Acetic Acid;Nature;1961-01

2. AUXIN-PROTEIN COMPLEXES OF THE WHEAT GRAIN;American Journal of Botany;1946-03

3. Wheat Gluten;Advances in Protein Chemistry;1945

4. Solubility of Gluten;Nature;1934-09

5. PREPARATION AND HEAT DENATURATION OF THE GLUTEN PROTEINS;Canadian Journal of Research;1931-10-01

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