PRODUCTION OF HUMAN MATRIX METALLOPROTEINASE-3 (STROMELYSIN) IN ESCHERICHIA-COLI

Full-length human matrix metalloproteinase 3 (prostromelysin or proMMP -3) was produced in Escherichia coli as an intracellular insoluble agg regate that could be solublized and refolded to yield an activatable p roenzyme. The refolded protein was purified to >95% homogeneity. The r ecombinant proMMP-3 (re-proMMP-3) could be activated by agents known t o stimulate self-catalyzed cleavage of native fibroblast proMMP-3. The N-terminal amino-acid sequence of the re-proMMP-3 and its activation products indicated that they were the same as those obtained with the natural material.