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

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

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Abstract

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 +/.

Publication Date:: Sun Jan 05 00:00:00 EST 1986

Research Org.:: Kyoto Univ., Japan

OSTI Identifier:: 5179105

Resource Type:: Journal Article

Journal Name:: J. Biol. Chem.; (United States)

Additional Journal Information:: Journal Volume: 261:1

Country of Publication:: United States

Language:: English

Subject:: 59 BASIC BIOLOGICAL SCIENCES; 63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.; PHOSPHORYLATION; BIOCHEMICAL REACTION KINETICS; PROTEINS; RETINA; ZINC COMPOUNDS; BIOLOGICAL EFFECTS; AMP; CATIONS; EXPERIMENTAL DATA; FROGS; INHIBITION; LABELLED COMPOUNDS; MAGNESIUM COMPOUNDS; MANGANESE COMPOUNDS; MOLECULAR WEIGHT; NUCLEOTIDES; PHOSPHORUS 32; PHOSPHOTRANSFERASES; SERINE; TRACER TECHNIQUES; ALKALINE EARTH METAL COMPOUNDS; AMINO ACIDS; AMPHIBIANS; ANIMALS; AQUATIC ORGANISMS; BETA DECAY RADIOISOTOPES; BETA-MINUS DECAY RADIOISOTOPES; BODY; BODY AREAS; CARBOXYLIC ACIDS; CHARGED PARTICLES; CHEMICAL REACTIONS; DATA; DAYS LIVING RADIOISOTOPES; ENZYMES; EYES; FACE; HEAD; HYDROXY ACIDS; INFORMATION; IONS; ISOTOPE APPLICATIONS; ISOTOPES; KINETICS; LIGHT NUCLEI; NUCLEI; NUMERICAL DATA; ODD-ODD NUCLEI; ORGANIC ACIDS; ORGANIC COMPOUNDS; ORGANS; PHOSPHORUS ISOTOPES; PHOSPHORUS-GROUP TRANSFERASES; RADIOISOTOPES; REACTION KINETICS; SENSE ORGANS; TRANSFERASES; TRANSITION ELEMENT COMPOUNDS; VERTEBRATES; 550201* - Biochemistry- Tracer Techniques; 560305 - Chemicals Metabolism & Toxicology- Vertebrates- (-1987)

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                    . Cyclic nucleotide-dependent phosphorylation of proteins in rod outer segments in frog retina: characteristics of the phosphorylated proteins and their dephosphorylation.  United States: N. p., 1986. 
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                    . Cyclic nucleotide-dependent phosphorylation of proteins in rod outer segments in frog retina: characteristics of the phosphorylated proteins and their dephosphorylation.  United States.

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                    . 1986.  
        "Cyclic nucleotide-dependent phosphorylation of proteins in rod outer segments in frog retina: characteristics of the phosphorylated proteins and their dephosphorylation".  United States.

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@article{osti_5179105,

  title        = {Cyclic nucleotide-dependent phosphorylation of proteins in rod outer segments in frog retina: characteristics of the phosphorylated proteins and their dephosphorylation},

  author       = {},

  abstractNote = {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 +/.},

  doi          = {},

  url          = {https://www.osti.gov/biblio/5179105},
  journal      = {J. Biol. Chem.; (United States)},
number       = ,

  volume       = 261:1,

  place        = {United States},

  year         = {Sun Jan 05 00:00:00 EST 1986},

  month        = {Sun Jan 05 00:00:00 EST 1986}

}

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