TY - JOUR
T1 - Inhibition of the mutagenicity of amino acid pyrolysis products by hemin and other biological pyrrole pigments
AU - Arimoto, Sakae
AU - Ohara, Yoshiko
AU - Namba, Takako
AU - Negishi, Tomoe
AU - Hayatsu, Hikoya
N1 - Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
PY - 1980/1/29
Y1 - 1980/1/29
N2 - 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.
AB - 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.
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U2 - 10.1016/0006-291X(80)90384-8
DO - 10.1016/0006-291X(80)90384-8
M3 - Article
C2 - 6986874
AN - SCOPUS:0018867523
SN - 0006-291X
VL - 92
SP - 662
EP - 668
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -