PMID: 8951420Dec 1, 1996Paper

Degradation of DMPO adducts from hydroxyl and 1-hydroxyethyl radicals by rat liver microsomes

Free Radical Research
L A ReinkeP B McCay

Abstract

Hydroxyl and 1-hydroxyethyl radical adducts of 5,5-dimethylpyrroline N-oxide (DMPO) were prepared by photolysis, and mechanisms for loss of their EPR signals in rat liver microsomal suspensions were evaluated. Rates of NADPH-dependent EPR signal loss were more rapid in phosphate buffer than in Tris buffer. Addition of superoxide dismutase (SOD) partially protected the adducts when Tris was used as a buffer, but was relatively ineffective in the presence of phosphate. The ferrous iron chelator bathophenan-throlene partially protected the spin adducts in the presence and absence of phosphate, but complete protection was observed when SOD was also added. The spin adducts were unstable in the presence of Fe+2 and K3Fe(CN)6, but Fe+3 alone had little effect on the EPR signals. The data are consistent with two mechanisms for microsomal degradation of DMPO spin adducts under these conditions. Microsomes from superoxide in the presence of oxygen and NADPH, which attacks these DMPO spin adducts directly. The spin adducts are also degraded in the presence of Fe+2, and phosphate stimulates this iron-dependent destruction of DMPO spin adducts.

References

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Apr 1, 1994·Free Radical Biology & Medicine·L A ReinkeP B McCay

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Citations

Feb 27, 2007·Free Radical Biology & Medicine·Griselda R BorthiryCharles R Myers
May 1, 2012·Free Radical Biology & Medicine·Charles R Myers
Oct 29, 2013·Free Radical Biology & Medicine·Nicolas BézièreFabienne Peyrot
Dec 9, 1997·Archives of Biochemistry and Biophysics·L A ReinkeP B McCay
Oct 25, 2016·Methods : a Companion to Methods in Enzymology·Kahina AbbasFabienne Peyrot

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