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

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.

journal_name

Free Radic Res

journal_title

Free radical research

authors

Reinke LA,Moore DR,McCay PB

doi

10.3109/10715769609149069

subject

Has Abstract

pub_date

1996-12-01 00:00:00

pages

467-74

issue

6

eissn

1071-5762

issn

1029-2470

journal_volume

25

pub_type

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