Regulation of phosphatase synthesis by orthophosphate in cultured tobacco cells

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Abstract
Phosphatase activity in cultured tobacco cells XD-6 increased remarkably under phosphate-deficient culture conditions. Such an increase did not occur in the activities of α-amylase, β-galactosidase, succinate dehydrogenase and catalase under the same culture conditions. By replenishment with Pi, the increase in total phosphatase activity was suppressed and the specific activity was reduced to a low level. The suppression of increase in the activity resulted form a repression of de novo synthesis of the enzyme. Added Pi also suppressed the release of phosphatase into the culture medium. The effect of Pi was found to be greater than the effect on the increase in the intracellular activity. At least three phosphatases were extracted from XD-6 cells. One of the enzymes increased when the phosphatase synthesis was increased by phosphate deficiency.