Plant Physiol. Drug Metab Dispos
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Plant Physiology 71:169-172 (1983)
© 1983 American Society of Plant Biologists

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Volume Regulation in Poterioochromonas1

Involvement of Calmodulin in the Ca2+-Stimulated Activation of Isofloridoside-Phosphate Synthase

Heinrich Kauss

Fachbereich Biologie der Universität, Postfach 3049, 6750 Kaiserslautern, Federal Republic of Germany

In Poterioochromonas malhamensis Peterfi (syn. Ochromonas malhamensis Pringsheim) osmotically induced shrinkage is reversed by an accumulation of isofloridoside. Addition of Ca2+ ions to homogenates from standard volume cells initiates an enzyme system for the activation of isofloridoside-phosphate synthase. This process is stimulated in the presence of Ca2+ by calmodulin, isolated from the same alga or from bovine brain, and requires the presence of membranes. The stimulation observed when Ca2+ is added without exogenous calmodulin is inhibited by the calmodulin-binding substance R 24571. These results show that the effect of Ca2+ is mediated by calmodulin. The Ca2+/calmodulin-dependent activation is enhanced when fluoride or molybdate ions are present in the homogenization buffer. This might indicate the involvement of a phosphorylated compound in the activation mechanism.


1 This work was supported by a grant from the Deutsche Forschungs-gemeinschaft.




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K. VELUTHAMBI and B. W. POOVAIAH
Calcium-Promoted Protein Phosphorylation in Plants
Science, January 13, 1984; 223(4632): 167 - 169.
[Abstract] [PDF]




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Copyright © 1983 by the American Society of Plant Biologists