Prostaglandin H synthase-dependent epoxidation of aflatoxin B1

This report demonstrates that aflatoxin B1 (AFB1) is cooxidized by prostaglandin H (PGH) synthase to form 2,3-dihydro-2,3-epoxy-aflatoxin B1 oxide. Using ram seminal vesicle microsomes as a source of PGH synthase, our results demonstrate that AFB1 is converted to a mutagen during arachidonate turnov...

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Bibliographic Details
Published in:Carcinogenesis (New York) Vol. 6; no. 8; p. 1227
Main Authors: Battista, J R, Marnett, L J
Format: Journal Article
Language:English
Published: England 01-08-1985
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Summary:This report demonstrates that aflatoxin B1 (AFB1) is cooxidized by prostaglandin H (PGH) synthase to form 2,3-dihydro-2,3-epoxy-aflatoxin B1 oxide. Using ram seminal vesicle microsomes as a source of PGH synthase, our results demonstrate that AFB1 is converted to a mutagen during arachidonate turnover that we identify as the epoxide by isolating adducts formed to DNA. The efficiency of AFB1 epoxidation by PGH synthase is assessed and compared with mixed-function oxidase-dependent metabolic activation of this compound.
ISSN:0143-3334
DOI:10.1093/carcin/6.8.1227