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Inhibition of lipid peroxidation by heme-nonapeptide derived from cytochrome c

  • Lajos Vodnyánszky
  • , Attila Marton
  • , István Venekei
  • , Mikiós Végh
  • , Anna Blázovits
  • , Ágnes Kittel
  • , István Horváth

Research output: Journal Publications and Reviews › RGC 21 - Publication in refereed journal › peer-review

Abstract

Heme-nonapeptide, derived from cytochrome c, inhibited both the NADPH- and NADH-dependent lipid peroxidation of brain microsomes but, in the case of liver microsomes, this inhibitory effect manifested itself in the presence of SKF-525A (a specific Mocker of cytochrome P-450) only. Heme-nonapeptide prevented the transient accumulation of lipid peroxides in microsomes during lipid peroxidation. The oxygen consumption of microsomes in the presence of NADPH or NADH was stimulated by heme-nonapeptide. From these results we concluded that, in vitro, there are two independent mechanisms of lipid peroxidation in liver microsomes. It is suggested that, in vivo, the heme-peptide-sensitive mechanism, observed in brain microsomes, is more important. © 1985.
Original languageEnglish
Pages (from-to)411-414
JournalBiochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism
Volume835
Issue number2
DOIs
Publication statusPublished - 9 Jul 1985
Externally publishedYes

Research Keywords

  • (Brain and liver microsome)
  • Heme-nonapeptide inhibitor
  • Lipid peroxidation
  • SKF-525A

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