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ouabain/helianthus
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Effect of high ionic strength and inhibitors of H,K-ATPase on the ouabain-sensitive K-p-nitrophenylphosphatase activity in the sea anemone Stichodactyla helianthus.
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The ouabain-sensitive, K-stimulated p-nitrophenyl phosphatase (K-pNPPase) activity, an associated activity of the Na,K-ATPase, was assayed in tentacles of the sea anemone Stichodactyla helianthus to investigate the possibility that the sea anemone Na,K-ATPase activity is an associated activity of an
An ouabain-sensitive Na+,K(+)-ATPase in tentacles of the sea anemone Stichodactyla helianthus.
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Tentacles of Stichodactyla helianthus contain an ouabain-inhibitable, (Na+,K+)-stimulated ATPase. The K0.5 for Na+ was 24 mM and for K+, 3.2 mM. The apparent affinity for ouabain was low, I50 = 10(-4) M. The order of cation affinities was Rb+ > K+ > NH4+ = Cs+. The catalytic subunit of the enzyme
A novel fluorescence imaging approach to monitor salt stress-induced modulation of ouabain-sensitive ATPase activity in sunflower seedling roots.
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Seedlings exposed to salt stress are expected to show modulation of intracellular accumulation of sodium ions through a variety of mechanisms. Using a new methodology, this work demonstrates ouabain (OU)-sensitive ATPase activity in the roots of sunflower seedlings subjected to salt stress (120 mM
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