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Inactivation of α 1 ‐antiproteinase by hydroxyl radicals The effect of uric acid
Author(s) -
Aruoma Okezie I.,
Halliwell Barry
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81166-4
Subject(s) - radical , chemistry , uric acid , hydroxyl radical , biochemistry , photochemistry , biophysics , biology
The elastase‐inhibitory activity of α,‐antiproteinase is inactivated by hydroxyl radicals ( . OH) generated by pulse radiolysis or by reaction of iron ions with H 2 O 2 in the presence of superoxide or ascorbate. Uric acid did not protect α 1 ‐antiproteinase against inactivation by . OH in pulse radiolysis experiments or in the superoxide/iron/H 2 O 2 system, whereas it did in systems containing ascorbic acid. We propose that radicals formed by attack of . OH on uric acid are themselves able to inactivate α 1 1 ‐antiproteinase, but that these uric acid radicals can be ‘repaired’ by ascorbic acid.