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Purified eNOS mutant protein has the same catalytic activity, the same rate to consume NADPH, and the same rate to generate superoxide as the wild-type eNOS. Wild-type and mutated eNOS expressed in COS-7 cells were purified. The activities (panel A), NADPH consumption (panel B), and superoxide generation (panel C) from these proteins were assayed as described under “Experimental Procedures.” Results are expressed as mean ± S.E.; n = 3 experiments. *, p < 0.05 versus vehicle group.
