1924 Observation aircraft family by Douglas.
1 Moreover, the mechanism and enzyme site responsible for O-2 generation is unknown.
2 Furthermore, strong O-2 generation was directly detected from the isolated iNOS reductase domain.
3 High concentrations of L-arginine decreased this O-2 formation, whereas its enantiomer D-arginine did not.
4 Conversely, pretreatment of the enzyme with the heme blocker cyanide had no effect on O-2 generation.
5 Products of the uncoupled reactions are analyzed using diacetyldeuteroheme-substituted horseradish peroxidase as a trapping agent for both O-2.
6 Our recent work has provided evidence that inducible NOS (iNOS) may also catalyze O-2 formation in macrophages.
7 Together, these data demonstrate that iNOS does generate O-2, and this mainly occurs at the flavin-binding sites of the reductase domain.
8 Further sulfation occurred either at O-3 or at O-2 of the GlcA residues, depending on the experimental conditions.
9 However, in these studies, DMTU did not scavenge O-2 and scavenged H2O2 only very slowly while scavenging OH very effectively.
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