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http://purl.uniprot.org/citations/12804606http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12804606http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12804606http://www.w3.org/2000/01/rdf-schema#comment"The heme and flavin-binding domains of Drosophila nitric oxide synthase (DNOS) were expressed in Escherichia coli using the expression vector pCW. The denatured molecular mass of the expressed protein was 152kDa along with a proteolytically cleaved product of 121kDa. The DNOS heme protein exhibited very low Ca(2+)/calmodulin-dependent NO synthase activity. The trypsin digestion patterns were different from nNOS. The full-length DNOS protein had high degree of stability against trypsin. The activity assay of trypsin-digested protein confirmed the same result. Urea dissociation profile of DNOS full-length protein showed that the reductase domain activity was much more susceptible towards urea than the oxygenase domain activity. Urea gradient gel of DNOS full-length protein established distinct transition of dissociation and unfolding in the range 3-4M urea. Reductase domain activity of full-length DNOS protein against external electron acceptors like cytochrome c indicated slow electron transfer from FMN. The bacterial expression of DNOS full-length protein represents an important development in structure-function studies of this enzyme and comparison with other mammalian NOS enzymes which is evolutionary significant."xsd:string
http://purl.uniprot.org/citations/12804606http://purl.org/dc/terms/identifier"doi:10.1016/s0006-291x(03)01003-9"xsd:string
http://purl.uniprot.org/citations/12804606http://purl.org/dc/terms/identifier"doi:10.1016/s0006-291x(03)01003-9"xsd:string
http://purl.uniprot.org/citations/12804606http://purl.uniprot.org/core/author"Ghosh S."xsd:string
http://purl.uniprot.org/citations/12804606http://purl.uniprot.org/core/author"Ghosh S."xsd:string
http://purl.uniprot.org/citations/12804606http://purl.uniprot.org/core/author"Mukherjee S."xsd:string
http://purl.uniprot.org/citations/12804606http://purl.uniprot.org/core/author"Mukherjee S."xsd:string
http://purl.uniprot.org/citations/12804606http://purl.uniprot.org/core/author"Regulski M."xsd:string
http://purl.uniprot.org/citations/12804606http://purl.uniprot.org/core/author"Regulski M."xsd:string
http://purl.uniprot.org/citations/12804606http://purl.uniprot.org/core/author"Sengupta R."xsd:string
http://purl.uniprot.org/citations/12804606http://purl.uniprot.org/core/author"Sengupta R."xsd:string
http://purl.uniprot.org/citations/12804606http://purl.uniprot.org/core/author"Tully T."xsd:string
http://purl.uniprot.org/citations/12804606http://purl.uniprot.org/core/author"Tully T."xsd:string
http://purl.uniprot.org/citations/12804606http://purl.uniprot.org/core/author"Stuehr D.J."xsd:string
http://purl.uniprot.org/citations/12804606http://purl.uniprot.org/core/author"Stuehr D.J."xsd:string
http://purl.uniprot.org/citations/12804606http://purl.uniprot.org/core/author"Sahoo R."xsd:string
http://purl.uniprot.org/citations/12804606http://purl.uniprot.org/core/author"Sahoo R."xsd:string
http://purl.uniprot.org/citations/12804606http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12804606http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12804606http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/12804606http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/12804606http://purl.uniprot.org/core/pages"590-597"xsd:string
http://purl.uniprot.org/citations/12804606http://purl.uniprot.org/core/pages"590-597"xsd:string