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Title: Cyclic nucleotide-dependent phosphorylation of proteins in rod outer segments in frog retina: characteristics of the phosphorylated proteins and their dephosphorylation

Journal Article · · J. Biol. Chem.; (United States)
OSTI ID:5179105

To clarify the function of cyclic nucleotides in rod outer segments (ROS) of frog retinas, the cyclic nucleotide-dependent phosphorylation and dephosphorylation of protein was studied. cGMP or cAMP with (..gamma..-/sup 32/P)ATP in the dark enhanced the phosphorylation of two ROS proteins with M/sub r/ = 10,500 (Band 1) and 8500 (Band 2) according to sodium dodecylsulfate-polyacrylamide gel electrophoresis analysis. The phosphorylation was maximally enhanced at 2.0 mM cGMP and cAMP in the presence of Mg/sup 2 +/. The cGMP-activated protein kinase showed near-optimal activity between pH 6.5 and 8.0. GMP, GDP, GTP, AMP, and ADP did not enhance the phosphorylation. Both /sup 32/P-phosphorylated Bands 1 and 2 were solubilized during preparation and the molecular weight of each was 19,000. Their isoelectric point was 5.2. The sites of phosphorylation were the serine residue(s). Dephosphorylation of /sup 37/P-Bands 1 and 2 in dark-adapted ROS suspension required Mn/sup 2 +/ or Mg/sup 2 +/. Both phosphorylation and dephosphorylation were inhibited by Zn/sup 2 +/.

Research Organization:
Kyoto Univ., Japan
OSTI ID:
5179105
Journal Information:
J. Biol. Chem.; (United States), Vol. 261:1
Country of Publication:
United States
Language:
English

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