Time kinetics of hemoglobin and myoglobin activation by tetrachlorodecaoxide (TCDO)

R. J. Youngman, G. R. Wagner, F. W. Kühne, E. F. Elstner

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

Abstract

In the presence of peroxidase, myoglobin or hemoglobin, Tetrachlorodecaoxide (TCDO) forms an active oxygen species which is similar to the product of the polymorphonuclear leucocyte (PMNL) myeloperoxidase reaction and the "Klebanoff Model" of phagocytosis, but it is also produced under anaerobic conditions. Randomly destructive species such as the free OH- radical or singlet oxygen are not formed. The kinetics of the heme-dependent activation vary according to the heme type present. In comparison to myoglobin, blood shows a 2 h delay in the appearance of maximal activity. On the basis of known biochemical and clinical-physiological data, a hypothesis can be proposed to explain the reoxygenation observed in hypoxic tissue, induced by TCDO via this activated heme species. Under normal physiological conditions, vasodilation occurs via catalysis by xanthine oxidase or PMNL-dependent activation of fatty acids.

Original languageEnglish
Pages (from-to)311-319
Number of pages9
JournalFree Radical Research
Volume1
Issue number5
DOIs
StatePublished - 1986

Keywords

  • Activated oxygen
  • Peripheral oxygen supply
  • Tetrachlorodecaoxide
  • Wound healing

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