Molecular characterization of the high-affinity [3H]neuropeptide Y-binding component from the venom of Conus anemone
Le, M.T.; Vanderheyden, P.M.L.; Fierens, F.L.P.; Vauquelin, G. (2003). Molecular characterization of the high-affinity [3H]neuropeptide Y-binding component from the venom of Conus anemone. Fundamental & Clinical Pharmacology 17(4): 457-462. https://dx.doi.org/10.1046/j.1472-8206.2003.00178.x
In: Fundamental & Clinical Pharmacology. Wiley-Blackwell: Hoboken. ISSN 0767-3981; e-ISSN 1472-8206, meer
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| Trefwoorden |
Conus anemone Lamarck, 1810 [WoRMS]
Marien/Kust |
| Author keywords |
Conus anemone; molecular weight; native PAGE; neuropeptide Y |
| Auteurs | | Top |
- Le, M.T.
- Vanderheyden, P.M.L.
- Fierens, F.L.P.
- Vauquelin, G.
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| Abstract |
The venom of the marine snail Conus anemone contains the ‘ANPY toxin’ which binds neuropeptide Y (NPY) and related insect peptides with nanomolar affinity. This toxin has initially been proposed to be a major 18.5 kDa component of the venom. Here we demonstrate that the 18.5 kDa proteins of venom produce at least five different bands in native electrophoresis and that none of them binds [3H]NPY. Instead, the ANPY toxin migrates as a distinct band on native electrophoresis and is only present as a minor component in the venom. Its approximate molecular weight is 17.5 kDa and its [3H]NPY binding activity is extremely stable below 37 °C, even in the absence of protease inhibitors. |
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