Stability of induced α-glucosidase activity in the absence of inducer

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Abstract
Yeast cells containing induced α-glucosidase activity lose 10% of the original activity per hour when placed in phosphate buffer – glucose medium. The presence of inducer has no effect on the rate of loss. Induced cells placed in complex medium plus glucose or glycerol show an initial rise in α-glucosidase activity, and then a slow decrease which is accelerated when growth stops. The loss of induced enzyme activity in buffer–glucose medium is inhibited by inhibitors of energy production or protein synthesis whether they are added immediately or 2 or 4 h after suspension of cells in the medium. The ability of the inhibitors to block the loss of induced enzyme activity is correlated with their ability to inhibit protein synthesis. Ammonium sulfate inhibits the loss of α-glucosidase activity after a lag but amino acid or purine–pyrimidine mixtures do not. The loss of induced enzyme activity in cell-free supernatant solutions is less than 2% of the original activity per hour at 30°.

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