Abstract
We have investigated changes in palmitate desaturation involving the quick cryoadaptation under inhibition of protein synthesis with actinomycin D or puromycin in Tetrahymena and provided evidence which supports at least in part the hypothesis of desaturase induction. The apparent turnover rates t 1 2 of palmitate desaturation activity were estimated at different growth temperatures in actinomycin D-treated cells with no induction of desaturase enzymes; approx. 40 min and 140–200 min at 39.5°C and 15°C, respectively, regardless of either pre-existing or induced desaturation activity. Taken together with data concerning the combined downward and upward temperature shifts, the observations obtained in this study lead us to postulate that, once synthesized, palmitoyl-CoA desaturase would be controlled by membrane fluidity of microsomes in Tetrahymena cells.
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