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- W2085496422 abstract "Pyrolyzates of 25 amino acids and 5 indole derivatives were tested for mutagenicity in the histidine-requiring mutant Salmonella typhimurium TA 98. Significant mutagenic activity was detected with pyrolyzates of most of the amino acids. These pyrolyzates required a liver microsomal fraction, as representative of mammalian metabolism, to be detected as mutagens. Among the pyrolyzates tested, the highest mutagenic activity was observed with that of L-tryptophan. As little as 10 μg of the pyrolyzate of L-tryptophan had detectable mutagenic activity toward TA 98. The optimal pyrolysis temperatures for the formation of mutagenic products were shown to be 500° C for L-tryptophan and 600° C for the other amino acids. The results from pyrolyses of some indole derivatives suggest that an amino group at the α-position to the carboxyl group of L-tryptophan plays an important role in the formation of mutagens." @default.
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- W2085496422 date "1977-07-01" @default.
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- W2085496422 title "Mutagenic activity of amino acid pyrolyzates in Salmonella typhimurium TA 98" @default.
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- W2085496422 doi "https://doi.org/10.1016/0027-5107(77)90170-1" @default.
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