Selective Fluorescence Detection of Small-Molecule-Binding Proteins by Using a Dual Photoaffinity Labeling System

ChemBioChem ◽  
2013 ◽  
Vol 14 (4) ◽  
pp. 421-425 ◽  
Author(s):  
Kaori Sakurai ◽  
Rika Yamada ◽  
Ayumi Okada ◽  
Masaki Tawa ◽  
Shimpei Ozawa ◽  
...  
Keyword(s):  
Small Molecule ◽  
Fluorescence Detection ◽  
Binding Proteins ◽  
Photoaffinity Labeling ◽  
Labeling System

Active/Inactive Dual‐Probe System for Selective Photoaffinity Labeling of Small Molecule‐Binding Proteins

2012 ◽  
Vol 7 (7) ◽  
pp. 1567-1571 ◽  
Author(s):  
Kaori Sakurai ◽  
Masaki Tawa ◽  
Ayumi Okada ◽  
Rika Yamada ◽  
Noriyuki Sato ◽  
...  
Keyword(s):  
Small Molecule ◽  
Binding Proteins ◽  
Photoaffinity Labeling ◽  
Probe System ◽  
Dual Probe

Photoaffinity Labeling of Small-Molecule-Binding Proteins by DNA-Templated Chemistry

2013 ◽  
Vol 125 (36) ◽  
pp. 9723-9728 ◽  
Author(s):  
Gang Li ◽  
Ying Liu ◽  
Yu Liu ◽  
Li Chen ◽  
Siyu Wu ◽  
...  
Keyword(s):  
Small Molecule ◽  
Binding Proteins ◽  
Photoaffinity Labeling

Photoaffinity Labeling of Small-Molecule-Binding Proteins by DNA-Templated Chemistry

2013 ◽  
Vol 52 (36) ◽  
pp. 9544-9549 ◽  
Author(s):  
Gang Li ◽  
Ying Liu ◽  
Yu Liu ◽  
Li Chen ◽  
Siyu Wu ◽  
...  
Keyword(s):  
Small Molecule ◽  
Binding Proteins ◽  
Photoaffinity Labeling

scholarly journals Small-Molecule Ligands of Methyl-Lysine Binding Proteins

2011 ◽  
Vol 54 (7) ◽  
pp. 2504-2511 ◽  
Author(s):  
J. Martin Herold ◽  
Tim J. Wigle ◽  
Jacqueline L. Norris ◽  
Robert Lam ◽  
Victoria K. Korboukh ◽  
...  
Keyword(s):  
Small Molecule ◽  
Binding Proteins ◽  
Small Molecule Ligands

Hemolymph juvenile hormone binding proteins of lepidopterous larvae: Enantiomeric selectivity and photoaffinity labeling

1987 ◽  
Vol 17 (4) ◽  
pp. 551-560 ◽  
Author(s):  
Glenn D. Prestwich ◽  
Steven Robles ◽  
Czeslaw Wawrzeńczyk ◽  
Adrian Bühler
Keyword(s):  
Juvenile Hormone ◽  
Binding Proteins ◽  
Photoaffinity Labeling ◽  
Hormone Binding ◽  
Enantiomeric Selectivity

Enhancement by GTP of cAMP binding to hepatic nuclei and cytosol

1984 ◽  
Vol 246 (1) ◽  
pp. C131-C140 ◽  
Author(s):  
E. M. Rosenberg ◽  
A. D. Goodman ◽  
T. L. Lipinski
Keyword(s):  
Binding Proteins ◽  
Specific Binding ◽  
Photoaffinity Labeling ◽  
Deae Cellulose ◽  
Nuclear Extract ◽  
Liver Cytosol ◽  
Nuclear Binding ◽  
Low Concentrations ◽  
Relative Molecular Weight

In the present study we have demonstrated specific binding of 3H-labeled adenosine 3',5'-cyclic monophosphate (cAMP) to a nuclear extract from rat liver. GTP, GDP, and low concentrations of ATP and ADP increased nuclear binding of [3H]cAMP, and AMP inhibited [3H]cAMP binding. Photoaffinity labeling studies employing [32P]cAMP revealed four nuclear binding proteins [relative molecular weight (Mr) 36,000, 49,000, 54,000 and 57,000]. Unlabeled cAMP decreased [32P]cAMP binding to all four proteins, whereas GTP increased binding to the 57,000 protein. We also observed specific binding of [3H]cAMP in the liver cytosol, which was stimulated by GTP but not by ADP or ATP. Photoaffinity labeling studies of the cytosol in the absence of unlabeled nucleotides revealed three cAMP-binding proteins (Mr 36,000, 49,000, and 54,000). Unlabeled cAMP inhibited binding of [32P]cAMP to all three proteins, whereas in the presence of GTP there was binding of [32P]cAMP to a Mr 57,000 protein. Using DEAE-cellulose, we isolated from the nuclear extract and cytosol a cAMP-binding protein that responded to GTP with an increase in cAMP binding but was unaffected by GDP, ATP, ADP, and AMP. Guanosine imidodiphosphate did not affect cAMP binding, suggesting that the stimulatory effect of GTP may be mediated by phosphorylation. We speculate that alterations in intracellular GTP in vivo may modulate the binding of cAMP to a protein in the nucleus and cytosol.

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