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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-2
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pubmed:dateCreated |
1998-9-23
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pubmed:abstractText |
Early work from our laboratory has shown that the mutagenicity of heterocyclic amines in Salmonella can be inhibited by hemin and chlorophyllins. We have speculated that the inhibition is a result of complex formation between heterocyclic amines and the pigments, and the speculation has been given a line of experimental evidence. We have now found that ferric-chlorophyllin (Fe-chlorophyllin) can modify the mutagenicity of 3-hydroxyamino-1-methyl-5H-pyrido[4, 3-b]indole (Trp-P-2(NHOH)), a metabolically activated form of 3-amino-1-methyl-5H-pyrido[4,3-b]indole (Trp-P-2). The mutagenicity of Trp-P-2(NHOH) in Salmonella typhimurium TA 98 (without S9) was strongly inhibited by an addition of an equimolar Fe-chlorophyllin in the pre-incubation mixture. Fe-chlorophyllin also inhibited the mutagenicity of 2-hydroxyamino-6-methyldipyrido[1,2-a:3',2'-d] imidazole (Glu-P-1(NHOH)). A rapid change in the UV spectrum of a mixture of Trp-P-2(NHOH) and Fe-chlorophyllin was observed. Analysis by high performance liquid chromatography showed that Trp-P-2(NHOH) was converted into 3-nitroso-1-methyl-5H-pyrido[4,3-b]indole (Trp-P-2(NO)), the mutagenic potency of which is a quarter of that of Trp-P-2(NHOH). Furthermore, the mutagenicity of Trp-P-2(NO), in turn, was inhibited by Fe-chlorophyllin. We conclude that the suppression of the mutagenicity of Trp-P-2(NHOH) is ascribable to the oxidative function of Fe-chlorophyllin, coupled with its ability to form complex formation with the planar surface of the heterocyclic amine molecules.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/3-hydroxyamino-1-methyl-5H-pyrido(4...,
http://linkedlifedata.com/resource/pubmed/chemical/Antimutagenic Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Carbolines,
http://linkedlifedata.com/resource/pubmed/chemical/Chlorophyllides,
http://linkedlifedata.com/resource/pubmed/chemical/Iron,
http://linkedlifedata.com/resource/pubmed/chemical/Nitroso Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/chlorophyllin
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0027-5107
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 1998 Elsevier Science B.V. All rights reserved.
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
400
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
259-69
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9685672-Aerobiosis,
pubmed-meshheading:9685672-Antimutagenic Agents,
pubmed-meshheading:9685672-Carbolines,
pubmed-meshheading:9685672-Chlorophyllides,
pubmed-meshheading:9685672-Iron,
pubmed-meshheading:9685672-Mutagenicity Tests,
pubmed-meshheading:9685672-Nitroso Compounds,
pubmed-meshheading:9685672-Salmonella typhimurium
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pubmed:year |
1998
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pubmed:articleTitle |
Iron-chlorophyllin-mediated conversion of 3-hydroxyamino-1-methyl-5H-pyrido[4,3-b]indole (Trp-P-2(NHOH)) into its nitroso derivative.
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pubmed:affiliation |
Faculty of Pharmaceutical Sciences, Okayama University, 1-1-1 Tsushima, Okayama 700, Japan. arimoto@cc.okayama-u.ac.jp
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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