1981
DOI: 10.1016/0014-5793(81)80114-7
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Formation of a thiobarbituric‐acid‐reactive substance from deoxyribose in the presence of iron salts

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Cited by 788 publications
(377 citation statements)
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“…Damage to lipids and deoxyribose by iron-EDTA and hydrogen peroxide was markedly inhibited by the addition of a range of hydroxyl radical scavengers, superoxide dismutase and catalase (table 2) but not by urea, albumin and heat-denatured catalase which were included as controls for non-specific effects. Heat-denatured superoxide dismutase, however, retained some activity in the deoxyribose and phospholipid systems as previously observed [8].…”
Section: Resultssupporting
confidence: 82%
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“…Damage to lipids and deoxyribose by iron-EDTA and hydrogen peroxide was markedly inhibited by the addition of a range of hydroxyl radical scavengers, superoxide dismutase and catalase (table 2) but not by urea, albumin and heat-denatured catalase which were included as controls for non-specific effects. Heat-denatured superoxide dismutase, however, retained some activity in the deoxyribose and phospholipid systems as previously observed [8].…”
Section: Resultssupporting
confidence: 82%
“…Heat-denatured superoxide dismutase did not totally lose its enzymic activity, as observed in [8], and this probably reflects recombination of released copper and protein to restore some dismutase activity.…”
Section: Discussionmentioning
confidence: 69%
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“…16 In their method the malonaldehyde arises as a product of deoxyribose degradation by the HO radical. The product in combination with thiobarbituric acid forms a colored (2:1) thiobarbituric acid-malonaldehyde adduct that absorbs at 532 nm in acid solution.…”
Section: Methodsmentioning
confidence: 99%