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Binding sites for 125I-neuropeptide Y (NPY) on membranes from bovine adrenal medulla
Ist Teil von
European journal of pharmacology, 1989-12, Vol.173 (2), p.115-119
Ort / Verlag
Amsterdam: Elsevier B.V
Erscheinungsjahr
1989
Quelle
Elsevier ScienceDirect Journals
Beschreibungen/Notizen
Bovine adrenal medulla membranes were examined for the presence of specific
125I-neuropeptide Y (
125I-NPY) binding sites using rapid centrifugation to measure the amount of bound ligand. Specific binding was determined from the difference between
125I-NPY bound in the presence and absence of 10
−7 M unlabeled NPY. The binding was saturable and reached equilibrium within 5 min at 0°C. Analysis of specific
125I-NPY binding using the LIGAND computer program indicated a best fit for a two site model with a K
d of 0.26 nM and a B
max of 12 fmol/mg protein for the high affinity site and a K
d of 170 nM and a B
max of 6 pmol/mg protein for the low affinity site. The rate of dissociation (k
−1) was 0.071/min with a
t
1
2
of 9 min. Displacement curves for avian or human pancreatic polypeptide revealed that these peptides displaced
125I-NPY from both sites with IC
50 values greater than 10 nM.