[Conformational changes during proteinase inhibitor proteins interaction with chymotrypsin].

Using CD-spectroscopy and fluorescent probe technique, the formation of complexes of chymotrypsin with two highly efficient protein inhibitors of plant origin, e. g. inhibitors from pea seeds and potato tubers, was studied. The CD spectra recorded during the formation of the enzyme--potato tuber inhibitor complexes suggest that the inhibitor molecule. This is correlated with the data on fluorescence of ANS coupled to the inhibitor and to the inhibitor--chymotrypsin complex. In case of the pea seed inhibitor the changes in the CD spectra during the complex formation can result from the changes in the environment of the disulfide bonds in the protein--inhibitor molecule.