@article{ref1,
title="Cytochromes P450 from Papilio polyxenes: Adaptations to host plant allelochemicals",
journal="Comparative biochemistry and physiology. C, Comparative pharmacology and toxicology",
year="1993",
author="Zumwalt, J.G. and Neal, J.J.",
volume="106",
number="1",
pages="111-118",
abstract="1. Papilio polyxenes, a caterpillar which feeds on xanthotoxin-containing plants, has cytochromes P450 that are six- to 100-fold less sensitive to the suicide substrate inhibitor, xanthotoxin, than cytochromes P450 from Manduca sexta, which does not survive on xanthotoxin-containing plants. 2. Xanthotoxin is a suicide substrate inhibitor of O-demethylation of p-nitroanisole by M. sexta microsomes but a reversible inhibitor of O-demethylation by P. polyxenes microsomes. 3. Aldrin epoxidation is irreversibly inhibited by xanthotoxin in both species. 4. Patterns of cross inhibition demonstrate that O-demethylase and aldrin epoxidase from both species and the P. polyxenes xanthotoxin-metabolizing cytochrome P450 are distinct enzymes. © 1993.<p /><p>Language: en</p>",
language="en",
issn="0742-8413",
doi="10.1016/0742-8413(93)90261-I",
url="http://dx.doi.org/10.1016/0742-8413(93)90261-I"
}