Interaction of Wheat Germ Ca 2+ -Dependent Protein Kinases with Calmodulin Antagonists and Polyamines

  • Polya G
  • Micucci V
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Abstract

The two soluble Ca(2+)-dependent protein kinases resolved from wheat (Triticum aestivum) embryo (protein kinases I and II) are inhibited by the phenothiazine-derived calmodulin antagonists trifluoperazine fluphenazine, and chlorpromazine. Protein kinases I and II are also inhibited by a variety of other calmodulin antagonists (including calmidazolium, amitriptyline, and iprindole), phosphodiesterase inhibitors (including flufenamic acid and papavarine) and by lanthanides. A number of compounds that inhibit mammalian Ca(2+) - and phospholipid-activated protein kinase (protein kinase C) including quercetin, polymixin B sulfate, and polyamines (as well as phenothiazine derivatives) also inhibit protein kinases I and II. Poly-l-lysine and poly-l-ornithine activate both plant Ca(2+)-dependent protein kinases.

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Polya, G. M., & Micucci, V. (1985). Interaction of Wheat Germ Ca 2+ -Dependent Protein Kinases with Calmodulin Antagonists and Polyamines. Plant Physiology, 79(4), 968–972. https://doi.org/10.1104/pp.79.4.968

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