PURIFICATION OF RECOMBINANT HUMAN PROSTROMELYSIN - STUDIES ON HEAT ACTIVATION TO GIVE HIGH-MR AND LOW-MR ACTIVE FORMS, AND A COMPARISON OF RECOMBINANT WITH NATURAL STROMELYSIN ACTIVITIES

Recombinant human prostromelysin was purified in a single step using Procion Red-Sepharose chromatography. The purified prostromelysin was self-activated to high-M(r) (45 000) and low-M(r) (28 000) forms by incubation at 55-degrees-C without the addition of extraneous activators. The two forms of stromelysin were subsequently separated, again using Procion Red-Sepharose. Both of the heat-activated recombinant forms demonstrated similar specific activities (for the macromolecular substrates casein, gelatin, elastin, proteoglycan and type IV collagen) when compared with either heat-or trypsin-activated natural stromelysin. The heat-activated recombinant stromelysins both showed similar abilities to potentiate activation of human procollagenase when compared with trypsin-activated natural stromelysin.