@article{LohseElgerLindenbornFotinosetal.1988,
  author    = {Lohse, M. J. and Elger, B. and Lindenborn-Fotinos, J. and Klotz, Karl-Norbert and Schwabe, U.},
  title     = {Separation of solubilized A\(_2\) adenosine receptors of human platelets from non-receptor [\(^3\)H]NECA binding sites by gel filtration},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-60309},
  year      = {1988},
  abstract  = {Human platelet membranes were solubilized with the zwitterionic detergent CHAPS (3-[3-(cholamidopropyl)dimethylammonio]- 1-propanesulfonate) and the solubilized extract subjected to gel ftltration. Binding of the adenosine receptor agonist [\(^3\)H]NECA (5'-N-ethylcarboxamidoadenosine) was measured to the eluted fractions. Two [\(^3\)H]NECA binding peaks were eluted, the first of them with the void volume. This first peak represented between 10\% and 25\% of the [\(^3\)H]NECA binding activity eluted from the column. It bound [\(^3\)H]NECA in a reversible, saturable and GTPdependent manner with an affinity of 46 nmol/1 and a binding capacity of 510 fmol/mg protein. Various adenosine receptor ligands competed for the binding of [\(^3\)H]NECA to the frrst peak with a pharmacological proftle characteristic for the A\(_2\) adenosine receptor as determined from adenylate cyclase experiments. In contrast, most adenosine receptor ligands did not compete for [\(^3\)H]NECA binding to the second, major peak. These results suggest that a solubilized A\(_2\) receptor-Gs protein complex of human platelets can be separated from other [\(^3\)H]NECA binding sites by gel filtration. This allows reliable radioligand binding studies of the A2 adenosine receptor of human plate1ets.},
  subject      = {Toxikologie},
  language  = {en}
}