EXPRESSION OF HUMAN INDUCIBLE NITRIC-OXIDE SYNTHASE IN ESCHERICHIA-COLI

We have expressed active full-length human inducible nitric oxide synt hase (iNOS) in E. coli. Expression required co-expression with calmodu lin, a particularly tight-binding cofactor. The extracts also required tetrahydrobiopterin to display activity, Specific activity of the pur ified recombinant iNOS was similar to iNOS purified from murine macrop hages. This result indicates that no special processing events unique to eucaryotic cells are necessary for iNOS activity.