Abstract
An NADPH 2-linked cytoplasmic enzyme system of duck liver reduces aflatoxin B 1 to the cyclopentenol, aflatoxicol. This reaction is readily reversible in vitro. While isolated liver microsomes contain an enzyme that hydrates the vinyl ether double bond of aflatoxin to form its hemiacetal, no such analogue of aflatoxicol is formed under the same incubation conditions. Any aflatoxins hemiacetal formed during prolonged incubations of aflatoxicol with crude liver preparations (9000 g supernatant) is derived indirectly from aflatoxin, the product of the reverse cytoplasmic reaction. Yields of hemiacetal are difficult to assess because of strong protein binding, which probably involves the formation of Schiff bases with free amino groups. Aflatoxin itself and aflatoxicol bind to protein less readily than does the hemiacetal.
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