EXPRESSION AND PURIFICATION OF HUMAN MATRILYSIN PRODUCED IN BACULOVIRUS-INFECTED INSECT CELLS

The baculovirus expression system was used to produce recombinant huma n matrilysin. Expression of promatrilysin reached a peak at 72 h post- infection. Most of the recombinant protein remained in the intracellul ar fraction in an insoluble form, which after renaturation was purifie d by S-Sepharose and Green A Dyematrex chromatography in order to remo ve host proteases. Active recombinant matrilysin degraded casein, type T and type IV collagens and fibronectin. Expression of recombinant hu man matrilysin using the baculovirus system represents a useful tool f or obtaining large amounts of this metalloproteinase in order to carry out further biochemical studies and to screen for inhibitors.