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The amounts of protein and the activities of the proteinase (trypsin) inhibitors of 16 varieties of pea have been studied. The amount of protein ranged from 19.3 to 25.2% and the amidase activities of the trypsin inhibitors from 18 to 40.8 IU. It was found that the electrophoretic spectrum of the inhibitor-containing fraction of the pea seed protein consisted of 12–16 components with molecular masses of 14–89 kDa. Features of the electrophoretic spectrum of some varieties of pea have been established.V. F. Kuprevich Institute of Experimental Botany, Belorussian SSR Academy of Sciences, Minsk. Translated from Khimiya Prirodnykh Soedinenii, No. 2, pp. 243–247, March–April, 1989.  相似文献   
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