Examination of the thermodynamic parameters and activation energies for the association of the Bowman‐Birk soybean proteinase inhibitor with trypsin and with chymotrypsin suggests that conformational changes may occur upon association. The data suggest that the nature of the two complexes may be somewhat different, and indicate that there is no pronounced interdependence of the kinetics, as well as the equilibria, for the sequential combination of the inhibitor with the two enzymes.
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