Effect of modification of cytochrome c on its reactions with superoxide and NADPH:cytochrome P-450 reductase |
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Authors: | E Finkelstein G M Rosen S E Patton M S Cohen E J Rauckman |
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Affiliation: | 1. Department of Pharmacology, Duke University Medical Center, Durham, North Carolina 27710 USA;2. Department of Surgery, Duke University Medical Center, Durham, North Carolina 27710 USA;3. Department of Medicine University of North Carolina, Chapel Hill, North Carolina 27514 USA.;4. Department of Bacteriology, University of North Carolina, Chapel Hill, North Carolina 27514 USA. |
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Abstract: | Acetylation and succinylation of cytochrome c decrease its rate of reaction with superoxide. The effect of succinylation is greater than that of acetylation. As predicted by the Brönsted-Debye-Hückel relationship, the effect of modification of cytochrome c is more pronounced at low ionic strength. Modification of cytochrome c causes a much greater decrease in its reaction with NADPH-cytochrome P-450 reductase, compared to its reaction with superoxide. This data forms the quantitative basis for the enhanced specificity of modified cytochrome c for superoxide detection previously described by other investigators. Additionally, a greatly simplified version of the trinitrobenzenesulfonic acid method for estimation of free amino groups is presented. |
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