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: Contribution to journalArticle

11 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)411-414
Number of pages4
JournalBiochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism
Issue number2
Publication statusPublished - Jul 9 1985


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

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Endocrinology

Fingerprint Dive into the research topics of 'Inhibition of lipid peroxidation by heme-nonapeptide derived from cytochrome c'. Together they form a unique fingerprint.

  • Cite this