Báo cáo khoa học: Unique features of recombinant heme oxygenase of Drosophila melanogaster compared with those of other heme oxygenases studied
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We cloned a cDNA for aDrosophila melanogasterhomo-logue ofmammalian heme oxygenase (HO) and constructed a bacterial expression system of a truncated, soluble form ofD. melanogasterHO (DmDHO). The purified DmDHO degraded hemin to biliverdin, CO and iron in the presence of reducing systems such as NADPH/cytochrome P450 reductase and sodium ascorbate, although the reaction rate was slower than that of mammalian HOs. Some properties of DmHO, however, are quite different from other known HOs.
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