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Tryptophan pyrolysate mutagenic activity

Yamazoe, Y., Ishii, K., Kamataki, T., Kato, R., and Sugimura, T., Isolation and characterization of active metabolites of tryptophan-pyrolysate mutagen, TRP-P-2, formed by rat liver microsomes, Chemico-Biol. Interact., 30, 125, 1980. [Pg.158]

Sugimura Isolation and characterization of active metabolites of tryptophan pyrolysate mutagen, Trp-P-2, 4386. [Pg.1434]

Significant mutagenic activity was detected with pyrolysates of most of the materials tested. The highest mutagenic activity was observed with pyrolysate of a tryptophan-containing peptide. The pyrolysates required a liver microsomal portion, representative of mammalian metabolism, for the detection of mutagens. [Pg.277]

Kosuge et described in detail the results of their investigation on the mutagenic activity of tars from amino acids, especially tryptophan. A series of amino acids were pyrolysed and fractionated, and the basic fractions from pyrolysates of tryptophan, ornithine, glutamic acid, serine, lysine, and creatine were shown to be mutagenic to 5. typhimurium TA98. Among the active principles in the... [Pg.277]


See other pages where Tryptophan pyrolysate mutagenic activity is mentioned: [Pg.524]    [Pg.524]    [Pg.556]    [Pg.522]    [Pg.122]    [Pg.130]    [Pg.43]    [Pg.409]   
See also in sourсe #XX -- [ Pg.524 ]




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