Effects of kinetin on phosphorylation of leaf membrane proteins.
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.
D002462:Cell Membrane / Q000187:drug effects / Q000201:enzymology / Q000648:ultrastructure; D002736:Chloroplasts / Q000187:drug effects / Q000201:enzymology / Q000648:ultrastructure; D007700:Kinetics; D007701:Kinetin / Q000494:pharmacology*; D010937:Plant Growth Regulators / Q000494:pharmacology*; D010940:Plant Proteins / Q000378:metabolism*; D010944:Plants / Q000187:drug effects / Q000201:enzymology*; D011494:Protein Kinases / Q000378:metabolism*
D010937:Plant Growth Regulators; D010940:Plant Proteins; D011494:Protein Kinases; D007701:Kinetin