Unique features of recombinant heme oxygenase of Drosophila melanogaster compared with those of other heme oxygenases studied

We cloned a cDNA for a Drosophila melanogaster homologue of mammalian heme oxygenase (HO) and constructed a bacterial expression system of a truncated, soluble form of D. melanogaster HO (DmΔHO). The purified DmΔHO degraded hemin to biliverdin, CO and iron in the presence of reducing systems such as...

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Veröffentlicht in:	European journal of biochemistry 2004-05, Vol.271 (9), p.1713-1724
Hauptverfasser:	Zhang, Xuhong, Sato, Michihiko, Sasahara, Masanao, Migita, Catharina T., Yoshida, Tadashi
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals biliverdin Catalysis Chromatography, High Pressure Liquid Deferoxamine - pharmacology DNA, Complementary - chemistry Drosophila melanogaster Drosophila melanogaster - enzymology heme oxygenase Heme Oxygenase (Decyclizing) - chemistry Heme Oxygenase (Decyclizing) - genetics Heme Oxygenase (Decyclizing) - metabolism Hemin - chemistry insect Molecular Sequence Data NADPH/cytochrome P450 reductase Recombinant Proteins - chemistry
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