Electrophoretic patterns of protein components extracted from soybean seed were studied. On the same variety of soybean harvested in different places, one in level ground and the other in high ground, the authors found that there was a certain difference between them in the electrophoresis pattern of globulin fraction. In the experiment, however, the environmental effect to the globulin fraction of parent seed protein seemed as inhereditable to that of child seed protein.

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The results of microbiological assay of 18 kinds of total amino acids in the crops mentioned in the subtitle including the milled or hulled products of these specimen were presented. The values obtained were examined under the light of existing literatures. The decreose of alanine values by milling or hulling throughout the specimen was remarkable.

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18 kinds of total amino acid in the crops mentioned in the subtitle grown in Japan were determined, whereby the microbiological assay method using lactic acid bacteria was employed throughout the study. When the values comprehending those appeared in Part 1 and 2 were surveyed, it was revealed that buckwheat belonging exceptionally to the family of Polygonaceae gave an amino acid pattern significantly differing in the several kinds of acid level from other subjects of Gramines conducted in the study. The necessity of further study to observe the botanical relationship from the amino acid of seeds or their protein was emphasized.

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It was observed that the spray-dried water-soluble protein of soybean meal processed at low temperature has a marked trypsin inhibitor activity and when it was fed to rats, the food intake and growth of rats were depressed.
Since the degree of growth retardation seemed to be related to the amount of trypsin inhibitor, the effect of heating on soybean protein in overcoming antitryptic activity and also availability of heat treated protein and acid-precipitated fraction of native protein for the growth of rats were investigated.
The antitryptic activity test in vitro showed that trypsin inhibitor activity was reduced to a level of 15% of the original protein by mild heating at 90°C, 30 min., pH 6.4, although the rate of inactivation of trypsin inhibitor was higher when heated in an alkaline medium.
As the results of rat growth experiment, the heat treated protein supported the growth of rats, and the acid-precipitated fraction which was actually low in content of trypsin inhibitor showed a higher protein availability.

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