The process of pressure-induced modification of horse liver alcohol dehydrogenase (HLADH) was followed by measuringin situ catalytic activity (up to 250 MPa), intrinsic fluorescence (–600 MPa) and modifications of FTIR spectra (up to 1000 MPa). The tryptophan fluor-escence measurements and the kinetic data indicated that the pressure-induced denaturation of HLADH was a process involving several transitions and that the observed transient states have characteristic properties of molten globules. .
