Inhibitory effect of myoglobin and hemoglobin on the direct-acting mutagenicity of protein pyrolysate heterocyclic amine derivatives

Sakae Arimoto, Yoshiko Ohara, Kazuyuki Hiramoto, Hikoya Hayatsu

Research output: Contribution to journalArticlepeer-review

17 Citations (Scopus)

Abstract

We have shown in our earlier reports (Arimoto et al., 1980a, b) that hemin and some other porphyrins can inhibit the mutagenicity in Salmonella of heterocyclic amines derived from cooking of proteins. A direct interaction between hemin and the mutagens was implicated on the basis of the observation that some of the mutagens were inactivated when they had been metabolically converted into direct-acting mutagens before the treatment with hemin. Hemin is a bound constituent of various proteins including hemoglobin and myoglobin, which are abundantly present in the blood and muscles, respectively. An interesting question is whether or not hemoglobin and myoglobin can inhibit the activities of the mutagenic heterocyclic amines.

Original languageEnglish
Pages (from-to)253-258
Number of pages6
JournalMutation Research Letters
Volume192
Issue number4
DOIs
Publication statusPublished - Dec 1987

Keywords

  • Cytochrome c
  • Hemoglobin
  • Heterocyclic amines
  • Myoglobin

ASJC Scopus subject areas

  • Medicine(all)

Fingerprint Dive into the research topics of 'Inhibitory effect of myoglobin and hemoglobin on the direct-acting mutagenicity of protein pyrolysate heterocyclic amine derivatives'. Together they form a unique fingerprint.

Cite this