Open AccessA Soybean Proteinase Inhibitor
Author(s) -
Harry John B.,
Steiner Robert F.
Publication year - 1970
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1970.tb01069.x
Subject(s) - proteinase inhibitor , enzyme , kinetics , chymotrypsin , trypsin , trypsin inhibitor , chemistry , biochemistry , kunitz sti protease inhibitor , association (psychology) , philosophy , epistemology , quantum mechanics , physics
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.