The β-bungarotoxin-binding protein from chick brain: binding sites for different neuronal K channel ligands co-fractionate upon partial purification |
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Authors: | R R Schmidt H Betz |
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Institution: | ZMBH, Universit?t Heidelberg, Im Neuenheimer Feld, FRG. |
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Abstract: | β-Bungarotoxin (β-Butx) is a presynaptically active neurotoxin which blocks neuronal A-type K+ channels. Here, the efficient solubilisation and about 300-fold purification of the β-Butx-binding protein from chick brain were achieved by detergent extraction at high ionic strength followed by chromatography on DEAE Affigel Blue, β-Butx Affigel 102 and wheat germ agglutinin Sepharose. Binding of 125I-labelled β-Butx to the purified protein was inhibited by two other K+ channel ligands, dendrotoxin I and mast cell-degranulating peptide. It is concluded that the β-Butx-binding protein is a member of a family of voltage-gated K+ channels which exhibit varying affinities for different polypeptide ligands. |
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Keywords: | β-Bungarotoxin Dendrotoxin Mast cell-degranulating peptide K+ channel (Chick brain) |
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