Stimulation of protein phosphorylations in frog rod outer segments by protein kinase activators. Suppression of light-induced changes in membrane current and cGMP by protein kinase C activators

Addition of protein kinase C activators to electropermeabilized frog rod photoreceptors enhances the phosphorylation of proteins with molecular masses of 54, 24, 19, 17, 12, and 11 kDa. The latter two correspond to components I and II, which are also phosphorylated by cyclic nucleotide-dependent pro...

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Veröffentlicht in:	The Journal of biological chemistry 1989-05, Vol.264 (15), p.8857-8864
Hauptverfasser:	BINDER, B. M, BREWER, E, BOWNDS, M. D
Format:	Artikel
Sprache:	eng
Schlagworte:	8-Bromo Cyclic Adenosine Monophosphate - pharmacology Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Cell Membrane - physiology Cyclic GMP - analogs & derivatives Cyclic GMP - metabolism Cyclic GMP - pharmacology Diglycerides - pharmacology Enzyme Activation Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Glycerides - pharmacology Kinetics Light Membrane Potentials Molecular Weight Oleic Acid Oleic Acids - pharmacology Phosphoproteins - isolation & purification Phosphorylation Photoreceptor Cells - metabolism photoreceptors protein kinase protein kinase C Protein Kinase C - metabolism Protein Kinases - metabolism Proteins - metabolism Rana catesbeiana rhodopsin kinase Rod Cell Outer Segment - metabolism Tetradecanoylphorbol Acetate - pharmacology Transferases
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