THE FLUORESCENCE QUENCHING RESOLVED SPECTRA AND RED-EDGE EXCITATION FLUORESCENCE MEASUREMENTS OF HUMAN ALPHA-1-PROTEINASE INHIBITOR

The human alpha-1-proteinase inhibitor (alpha-1-PI) and its reactive site modified form (alpha-1-PI*) have been examined using the fluorescence quenching resolved spectra method. The red-edge excitation measurements were applied for the study of structural differences between these forms. The crystallographic data of alpha-1-PI* structure have shown that its polypeptide chain includes only two tryptophan residues. The fluorescence quenching data have indicated that the conversion of the intact inhibitor molecule into its nicked form is accompanied by changes in the tryptophan environments. The red-edge excitation measurements have proved that the dipolar relaxation process around the Trp-194 residue is much bigger in alpha-1-PI* form than in the nicked one.