title: Studies on the orientation of cyclic AMP-dependent protein kinase in human erythrocyte membranes.
abstract: The topographic location of cyclic AMP-dependent protein kinase has been studied in preparations of permeable and sealed membranes derived from human erythrocytes. Both the catalytic and cyclic AMP-binding components of protein kinase are localized on the inner, cytoplasmic, surface of the plasma membrane.
mesh_terms: D000110:Acetylcholinesterase / Q000097:blood; D001665:Binding Sites; D002384:Catalysis; D002462:Cell Membrane / Q000201:enzymology; D000242:Cyclic AMP / Q000097:blood* / Q000378:metabolism; D008058:Dihydrolipoamide Dehydrogenase / Q000097:blood; D004912:Erythrocytes / Q000166:cytology / Q000201:enzymology*; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000097:blood; D006801:Humans; D010761:Phosphorus Radioisotopes; D011485:Protein Binding; D011494:Protein Kinases / Q000097:blood* / Q000378:metabolism; D014316:Tritium
chemical_list: D010761:Phosphorus Radioisotopes; D014316:Tritium; D000242:Cyclic AMP; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D008058:Dihydrolipoamide Dehydrogenase; D011494:Protein Kinases; D000110:Acetylcholinesterase