A plant metabolic activation system from Persea americana with cytochrome P450-dependent and peroxidase activities.

Microsomal fractions from different tissues of various plants (potato, cauliflower, aubergine, avocado pear, courgette, cucumber, banana, kiwi and strawberry) were prepared and their content of cytochrome P-450 (cyt-P450) determined. A S117 fraction from Persea americana (avocado pear) presented the highest content of cyt-P450. As a consequence of these data, we have developed and characterized this fraction as a plant metabolic activation system. The P. americana S117, used in this work, contains 0.75 +/- 0.04 mg of protein per ml, 0.788 +/- 0.078 nmol of cyt-P450 per mg of protein and has a peroxidase activity of 0.036 +/- 0.005 (nmol tetraguaiacol/micrograms protein/min). The P. americana cyt-P450 remained stable during at least 60 days, stored at -80 degrees C. This fraction activated 2-aminofluorene to a mutagenic product in S. typhimurium TA98, while it had no effect on the benzo[a]pyrene activation. The treatment of the P. americana S117 with CO, the addition of diethyldithiocarbamate (DETC) or the absence of a NADPH-generating system in the activation mix, produced a partial inhibition of the 2-aminofluorene activation. Both peroxidase activity and a cyt-P450-dependent activity are assumed to be involved in the activation of this chemical mediated by P. americana S117.