Molecular characterization of the high-affinity [3H]neuropeptide Y-binding component from the venom of Conus anemone.
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 degrees C, even in the absence of protease inhibitors.
Le
Minh Tam
MT
Department of Molecular and Biochemical Pharmacology, Institute for Molecular Biology and Biotechnology, Free University of Brussels (VUB), Pleinlaan 2, 1050 Brussel, Belgium. tmleminh@vub.ac.be
Vanderheyden
Patrick M L
PM
Fierens
Frederik L P
FL
Vauquelin
George
G
D020916:Conotoxins / Q000737:chemistry* / Q000302:isolation & purification; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D008978:Mollusk Venoms / Q000737:chemistry*; D009478:Neuropeptide Y / Q000037:antagonists & inhibitors* / Q000378:metabolism; D011485:Protein Binding; D011869:Radioligand Assay; D013696:Temperature
D020916:Conotoxins; D008978:Mollusk Venoms; D009478:Neuropeptide Y