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Inhibition of autoxidation of divicine and isouramil by the combination of superoxide dismutase and reduced glutathione.

Abstract：

:The effects of GSH on the autoxidation of the fava bean pyrimidine aglycones, divicine and isouramil, and on acid-hydrolyzed vicine (provisional identification 2-amino-4,5,6-trihydroxypyrimidine) have been studied. GSH alone promoted redox cycling of each compound, with concomitant GSH oxidation and H2O2 production. In the presence of superoxide dismutase, there is a lag period during which little pyrimidine oxidation occurs, followed by a period of accelerated oxidation. With the three pyrimidines, increasing concentrations of GSH extended this lag period and progressively decreased subsequent rates of both pyrimidine oxidation and O2 uptake. No GSH oxidation or O2 uptake occurred during the lag. These results show that the combination of GSH and superoxide dismutase is able to inhibit redox cycling of the pyrimidines. With a 10-fold excess of GSH over isouramil or acid-hydrolyzed vicine (20-fold with divicine) this coupled oxidation of GSH and the pyrimidine is almost completely suppressed. This mechanism may be a means whereby GSH in combination with superoxide dismutase protects against the cytotoxic effects of these reactive pyrimidines.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Winterbourn CC

doi

10.1016/0003-9861(89)90295-6

subject

Has Abstract

pub_date

1989-06-01 00:00:00

pages

447-55

issue

2

eissn

0003-9861

issn

1096-0384

pii

0003-9861(89)90295-6

journal_volume

271

pub_type

杂志文章

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