Abstract
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.
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Additional information
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.
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Domash, V.I., Koroleva, O.S. & Kotlovskaya, G.N. Protein content, activity, and electrophoretic composition of the inhibitor-containing fraction of pea seeds. Chem Nat Compd 25, 210–213 (1989). https://doi.org/10.1007/BF00598414
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DOI: https://doi.org/10.1007/BF00598414