| Literature DB >> 8635578 |
J D Fossetta1, X D Niu, C A Lunn, P J Zavodny, S K Narula, D Lundell.
Abstract
We have expressed active full-length human inducible nitric oxide synthase (iNOS) in E. coli. Expression required co-expression with calmodulin, a particularly tight-binding cofactor. The extracts also required tetrahydrobiopterin to display activity. Specific activity of the purified recombinant iNOS was similar to iNOS purified from murine macrophages. This result indicates that no special processing events unique to eucaryotic cells are necessary for iNOS activity.Entities:
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Year: 1996 PMID: 8635578 DOI: 10.1016/0014-5793(95)01496-9
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124