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Reversible oxidation of glyceraldehyde 3-phosphate dehydrogenase thiols in human lung carcinoma cells by hydrogen peroxide.

Abstract：

:Human lung carcinoma cells (A549) were oxidatively stressed with mildly-toxic or non-toxic amounts of hydrogen peroxide (H2O2, 0.1 mM to 120 mM) for 5 min. Hydrogen peroxide exposure resulted in a dose dependent inhibition of binding (pH 7) of the thiol reagent iodoacetic acid (IAA) to a 38 kDa cell protein. Incubation of cells in saline for 60 min following H2O2 removal restored the ability of IAA to bind to the protein. Treatment with 20 mM dithiothreitol or 2 M urea also restored IAA binding, but 10% Triton X102 or 1 mM Brij 58 had no effect. Increasing to pH 11 during the IAA binding also increased thiol availability. Glyceraldehyde 3-phosphate dehydrogenase (EC 1.2.1.12) has been identified as the protein undergoing thiol/disulfide redox status and enzymic activity changes.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Brodie AE,Reed DJ

doi

10.1016/0006-291x(87)91084-9

subject

Has Abstract

pub_date

1987-10-14 00:00:00

pages

120-5

issue

1

eissn

0006-291X

issn

1090-2104

pii

0006-291X(87)91084-9

journal_volume

148

pub_type

杂志文章

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