A kinetic analysis of arylamine acetyltransferase activation by prodigiozane, a stimulator of organism unspecific resistance, has been carried out. The change of enzyme activity is associated not with a change of its tissue content, but is due to the appearance of a new isoenzyme with altered rate of product dissociation from the catalytic site under condition when k-1 much greater than kKaT. The effect observed is suggested to be defined by a genetically determined adaptative mobility of organism rather than by genetically determined enzyme synthesis. A search strategy for arylamine acetyltransferase activity regulators is proposed.
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