Cyclic AMP-protein-DNA complex formation in mammalian cell-free systems.
A cytoplasmic protein fraction from KB and Chinese hamster ovary cells (CHO-Kl) was shown to bind in vitro to cAMP and subsequently to DNA-cellulose. This protein complex was not found in DE-52 purified CHO-K1 cAMP-dependent protein kinases. The complex appeared to exist as a small fraction of the total cAMP binding proteins, preferred native to denatured DNA and exhibited multiple sedimentation coefficients in glycerol gradients. This complex, after elution from the DNA cellulose column, was shown to have bound specifically to [3H]-cAMP which could be displaced by non-radioactive cAMP in competitive binding assays.
D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism*; D002474:Cell-Free System; D002478:Cells, Cultured; D002482:Cellulose; D002846:Chromatography, Affinity; D006224:Cricetinae; D000242:Cyclic AMP / Q000378:metabolism*; D003600:Cytosol / Q000201:enzymology*; D004247:DNA / Q000378:metabolism*; D006801:Humans; D009711:Nucleotides / Q000378:metabolism; D009712:Nucleotides, Cyclic / Q000378:metabolism; D011485:Protein Binding; D011494:Protein Kinases / Q000032:analysis / Q000302:isolation & purification
D002352:Carrier Proteins; D009711:Nucleotides; D009712:Nucleotides, Cyclic; D002482:Cellulose; D004247:DNA; D000242:Cyclic AMP; D011494:Protein Kinases