Inhibition of the mutagenicity of amino acid pyrolysis products by hemin and other biological pyrrole pigments

Sakae Arimoto, Yoshiko Ohara, Takako Namba, Tomoe Negishi, Hikoya Hayatsu

Research output: Contribution to journalArticlepeer-review

136 Citations (Scopus)

Abstract

Inhibition of the mutagenic activities of the amino acid pyrolysis products by hemin and other biological pyrrole pigments was investigated using the Ames' Salmonella/microsome system. Hemin, biliverdin and chlorophyllin showed inhibition to all the six mutagens tested, and protoporphyrin to three of them. Hemin was the most effective among these pigments; e.g., the mutageniciti of 1.8 nmole Trp-P-1 (3-amino-1,4-dimethyl-5H-pyrido[4,3-b]indole) was suppressed to 50 % by 1-3 nmole of hemin. Hemin appears to interact with the metabolically activated form of Trp-P-1 and as a result to inhibit the mutagenicity.

Original languageEnglish
Pages (from-to)662-668
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume92
Issue number2
DOIs
Publication statusPublished - Jan 29 1980

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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