High-affinity binding of [3H]neuropeptide Y to a polypeptide from the venom of Conus anemone
Czerwiec, E.; De Backer, J.-P.; Vauquelin, G.; Vanderheyden, P.M.L. (1996). High-affinity binding of [3H]neuropeptide Y to a polypeptide from the venom of Conus anemone. European Journal of Pharmacology 315(3): 355-362. https://dx.doi.org/10.1016/S0014-2999(96)00647-4
In: European Journal of Pharmacology. ELSEVIER SCIENCE BV: Amsterdam. ISSN 0014-2999; e-ISSN 1879-0712, more
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| Keywords |
Conus anemone Lamarck, 1810 [WoRMS]
Marine/Coastal |
| Author keywords |
neuropeptide Y (NPY); (Conus anemone); binding protein; pancreaticpolypeptide; neuropeptide Y-(18-36) |
| Authors | | Top |
- Czerwiec, E.
- De Backer, J.-P.
- Vauquelin, G.
- Vanderheyden, P.M.L.
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| Abstract |
Venom preparation from Conus anemone contains a component that binds radiolabeled neuropeptide Y ([3H]neuropeptide Y) with high affinity (KD = 2.9 nM ± 0.2 nM, Bmax = 15.2 ± 0.5 pmol/mg protein). Binding of [3H]neuropeptide Y to the venom component is displaced with nanomolar affinity of unlabeled human and porcine neuropeptide Y, porcine [Leu31-Pro34]neuropeptide Y, peptide YY, avian and bovine pancreatic polypeptide, and the (18–36) and (25–36) C-terminal fragments from neuropeptide Y. No displacement is found with the (1–24) N-terminal neuropeptide Y fragment, human secretin, porcine dynorphin A and Boc-DAKLI (Bolton Hunter coupled dynorphin A analog kappa ligand) nor with the non-peptide neuropeptide Y receptor antagonist BIBP3266. Gel filtration chromatography and denaturing (sodium dodecyl sulfate-polyacrylamide gel electrophoresis) show that the [3H]neuropeptide Y-binding component is very likely a single-chain polypeptide with a molecular mass of 18.5 kDa. |
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