Author(s): Ralph RK, Bullivant S, Wojcik SJ, Ralph RK, Bullivant S, Wojcik SJ
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Abstract Isolated Chinese cabbage leaf membranes were phosphorylated by membrane-associated protein kinase(s) in the presence or [gamma-32P]ATP. Membrane-associated 32P radioactivity appeared to be bound to membrane proteins. Both smooth cell membranes and chloroplast lamellae reacted with ATP. Phosphorylation of the membranes was inhibited by Ca2+ and partially inhibited by kinetin or 6-benzyladenine. The possibility that cytokinin effects on membrane phosphorylation might increase ion availability was investigated in vivo. It was found that Ca2+ could substitute for kinetin in the leaf disc expansion assay.
This article was published in Biochim Biophys Acta
and referenced in Journal of Biodiversity, Bioprospecting and Development