Proteinase inhibitor and electrophoretic inhibitor patterns of lentils.
1985
Weder J.K.P. | Mueller R. | Ildefonso Mato C. | Hegarty M.P.
Thirty-eight lentil samples (commercial cultivars and accessions from various lentil collections) were tested for inhibitor activities against bovine trypsin and chymotrypsin. A larger group with low inhibitor content (0.6-1.1 mg trypsin and 0.4-0.9 mg alpha-chymotrypsin inhibited/g of seed meal) and a number of samples with higher inhibitor content (up to 2.5 mg trypsin or 2.4 mg alpha-chymotrypsin inhibited/g) were demonstrated. Inhibition of human trypsin fell in the same range as that of bovine trypsin (80-100%), while human chymotrypsin was inhibited more effectively than the bovine enzyme (150-260%). Four isoinhibitors were demonstrated electrophoretically in all the samples, which are grouped into three genetically-controlled inhibitor pattern types: type A, with the most basic inhibitor predominating; type B, with the most basic and the most acidic inhibitor occurring in equal amounts; and type C, with the most acidic inhibitor predominating. Genetic similarity seems to be more responsible for both inhibitor content and inhibitor pattern type than does geographical provenance.
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