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Interaction of Wheat Germ Ca²⁺-Dependent Protein Kinases with Calmodulin Antagonists and Polyamines ¹

Department of Biochemistry, La Trobe University, Bundoora, Victoria, 3083, Australia

The two soluble Ca²⁺-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 Ca²⁺ - 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 Ca²⁺-dependent protein kinases.

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