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- W2086785016 abstract "Two inhibitors isolated from Macrotylom axillare seeds were found to be of the Bowman-Birk type, each inhibiting both trypsin and chymotrypsin with equimolar stoichiometry. Stable binary and ternary complexes of inhibitor-enzyme or inhibitor-trypsin-chymotrypsin were isolated by gel chromatography, confirming the presence of independent interaction sites for the two enzymes on the inhibitor. Partial specific proteolysis at low pH revealed that its Lys 24 -Ser 25 and Leu 50 -Ser 51 bonds were involved in the interaction with trypsin and chymotrypsin, respectively. Fragments with reactivity against trypsin (F-t) or chymotrypsin (F-c) were isolated after cleavage of the inhibitor with cyanogen bromide and pepsin. The inhibitory potency of each isolated fragment was enhanced by the presence of the other in reconstituted mixtures. Features of the circular dichroism spectra suggest that there is some conformational interaction between the two independent enzyme-specific domains of the inhibitor." @default.
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- W2086785016 date "1982-03-01" @default.
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- W2086785016 title "Properties of fragments prepared from bowman-birk inhibitors" @default.
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- W2086785016 doi "https://doi.org/10.1016/0167-4838(82)90238-2" @default.
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