Kołoczek H, Waśniowska A, Potempa J, Wasylewski Z
Department of Biochemistry, Jagiellonian University, Kraków, Poland.
Biochim Biophys Acta. 1991 Apr 9;1073(3):619-25. doi: 10.1016/0304-4165(91)90239-d.
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.
已使用荧光猝灭分辨光谱法对人α1-蛋白酶抑制剂（α1-PI）及其反应位点修饰形式（α1-PI*）进行了研究。采用红边激发测量来研究这些形式之间的结构差异。α1-PI结构的晶体学数据表明，其多肽链仅包含两个色氨酸残基。荧光猝灭数据表明，完整抑制剂分子向其切口形式的转化伴随着色氨酸环境的变化。红边激发测量证明，α1-PI形式中Trp-194残基周围的偶极弛豫过程比切口形式中的大得多。
