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eins, in general, usually contain larger proportions of proline and of glutamic acid than are found in animal proteins; also more arginine than is found in any of the animal proteins except the protamines, which contain as high as 85 per cent of this amino-acid. Of the twenty-five plant proteins which have thus far been hydrolyzed and studied from this standpoint, all contained leucine, proline, phenylalanine, aspartic acid, glutamic acid, tyrosine, histidine, and arginine; two gave no glycine; two others, no alanine; four contained no lysine; and one, no tryptophane. Zein, the principal protein of corn contains no glycine, lysine, or tryptophane. It is not sufficient to support animal life and promote growth, if used as an exclusive source for protein for food. THE EXTRACTION OF PROTEINS FROM PLANT TISSUES Since proteins are indiffusible, it is essential that the cell-walls of the tissue shall be thoroughly ruptured as the first step in any process for the extraction of these compounds from plant tissues. This is usually accomplished by grinding the material as finely as possible, preferably with the addition of sharp quartz sand, or broken glass, to aid in the tearing of the cell-wall material. The solvent to be used in extracting the proteins from this finely ground material depends upon the nature and solubility of the proteins which are present, and also upon whether it is desired to separate the proteins which may be present in the plant, during the process of the extraction. A glance at the scheme of classification of the proteins will show the following solubilities which serve as a guide to the procedure to be followed: (_a_) proteoses, albumins, and some globulins may be extracted with water; (_b_) globulins and most of the water-soluble proteins may be extracted by using a 10 per cent solution of common salt; (_c_) prolamines are extracted by 70-90 per cent alcohol; glutelins and prolamins dissolve in dilute acids or dilute alkali. A common procedure is to extract groups (_a_) and (_b_), using a 10 per cent salt solution as the solvent, and then to separate the albumins, globulins, etc., from this solution by suitable precipitants; then to treat the material with 80 per cent alcohol, to extract the prolamines; and finally with dilute alkali, to extract the glutelins. The dissolved proteins in each extract can be subsequently purified by dialysis, precipitation, etc. The insoluble pro
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