An analysis of two refolding routes for a C-terminally truncated human collagenase-3 expressed in Escherichia coli

We describe here the expression of a C-terminally truncated form of human p rocollagenase-3 in Escherichia coli. The protein was found almost exclusive ly in inclusion bodies that were solubilized and refolded by two separate m ethods and then purified on Ni-NTA agarose. The purified proenzyme could be activated with either trypsin or APMA and active enzyme could be purified on a peptidic hydroxamate affinity column. Competitive elution from the aff inity matrix yielded a highly purified preparation. (C) 2000 Academic Press .