Full-length human matrix metalloproteinase 3 (prostomelysin or proMMP-3) was produced in Escherichia coli as an intracellular insoluble aggregate that could be solubilized and refolded to yield an activatable proenzyme. The refolded protein was purified to > 95% homogeneity. The recombinant proMMP-3 (re-proMMP-3) could be activated by agents known to 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.
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