FOLDING-UNFOLDING KINETICS OF HUMAN $\alpha_1$-ANTITRYPSIN: CHARACTERIZATION OF A KINETIC INTERMEDIATE THAT IS BRANCHED TO THE NATIVE AND AGGREGATION FORM

Aggregation of human $\alpha$$_1$-antitrypsin ($\alpha$$_1$-AT) during folding occurs both in vitro and in vivo. In vivo aggregates of mutant $\alpha$$_1$-AT such as $M_{malton}$ (Phe52 deleted) and Z (Glu342 longrightarrowLys) variants have pathological consequences. In order to analyze the process of $\alpha$$_1$-AT aggregation in detail, the folding-unfolding kinetics of $\alpha$$_1$-AT was examined by monitoring intrinsic Trp fluorescence and ANS binding. (omitted)