Purification and subunit structure of a putative K sup + -channel protein identified by its binding properties for dendrotoxin I
- Centre National de la Recherche Scientifique, Nice (France)
The binding protein for the K{sup +}-channel toxin dendrotoxin I was purified from a detergent extract of rat brain membranes. The purification procedure utilized chromatography on DEAE-Trisacryl, affinity chromatography on a dendrotoxin-I-Aca 22 column, and wheat germ agglutinin-Affigel 10 with a final 3,800- to 4,600-fold enrichment and a recovery of 8-16%. The high affinity (K{sub d}, 40-100 pM) and specificity of the binding site are retained throughout the purification procedure. Analysis of the purified material on silver-stained NaDodSO{sub 4}/polyacrylamide gel revealed three bands of M{sub r} 76,000-80,000, 38,000 and 35,000. Interestingly, the binding site for {sup 125}I-labeled mast cell degranulating peptide, another putative K{sup +}-channel ligand from bee venom, which induces long-term potentiation in hippocampus, seems to reside on the same protein complex, as both binding sites copurify through the entire purification protocol.
- OSTI ID:
- 5406018
- Journal Information:
- Proceedings of the National Academy of Sciences of the United States of America; (USA), Vol. 85:13; ISSN 0027-8424
- Country of Publication:
- United States
- Language:
- English
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550201* - Biochemistry- Tracer Techniques