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. 1984 Oct;76(2):331-5.
doi: 10.1104/pp.76.2.331.

Physiological control of arginine decarboxylase activity in k-deficient oat shoots

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Physiological control of arginine decarboxylase activity in k-deficient oat shoots

N D Young et al. Plant Physiol. 1984 Oct.

Abstract

The effect of K-deficiency on the putrescine biosynthetic enzyme, arginine decarboxylase (ADC), was investigated by growing oat (Avena sativa L. var Victory) plants on a low-K, but otherwise complete nutrient medium in washed quartz sand for up to 18 days. Enzyme activity rose as the concentration of KCl was dropped to 0.6 millimolar or below. However, growth was not inhibited significantly at 0.6 millimolar KCl. ADC activity increased in the whole shoot of K-deficient oats throughout the period of 6 to 18 days, but remained constant in normal plants. At 18 days, ADC activity in entire K-deficient shoots was 6 times greater than in normal shoots, while in the first (oldest) leaf, ADC specific activity increased to more than 30 times the specific activity in the first leaf of normal plants. This effect was due to a moderate rise in total ADC activity in the first leaf between 6 and 18 days, accompanied by a significant decline in protein content. Replacing K(+) with Na(+) or Li(+) significantly inhibited the increase in ADC activity in K-deficient oats, while Rb(+) depressed the specific activity to a level below that in normal plants. An alternative putrescine biosynthetic enzyme, ornithine decarboxylase, was also examined. The specific activity of a pelletable form of the enzyme was increased 2-fold in the shoots of K-deficient oats.

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References

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