The involvement of superoxide anions in the autoxidation of various cofactors of cysteamine-oxygenase.
Mol Cell Biochem, 1975/12/31;9(3):149-54.
Dupré S, Federici G, Santoro L, Rossi Fanelli MR, Cavallini D
PMID: 172779
Impact factor: 3.842
Abstract
The reduction of tetranitroblue tetrazolium with cysteamine, mediated by a number of dyes, elemental sulphur, elemental selenium and selenide, under aerobic conditions, was inhibited to various extent upon addition of superoxide dismutase. A strict parallelism between the ability to produce O2- ions and the property of those compounds to act as cofactors for cysteamine-oxygenase, to yield hypotaurine, has been observed. Based on the fact that the autoxidation of cysteamine also gives rise to O2- formation, though to a minor extent, we propose a mechanism for cysteamine-oxygenase action. This mechanism was derived from the data obtained in the model system studied.
MeSH terms
Animals; Cattle; Cysteamine; Electron Transport; Erythrocytes; Kinetics; Nitroblue Tetrazolium; Oxidation-Reduction; Oxygenases; Superoxide Dismutase; Superoxides
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