Oligomeric properties of .alpha.-dendrotoxin-sensitive potassium ion channels purified from bovine brain

Neuronal acceptors for alpha-dendrotoxin (alpha-DTX) have recently been purified from mammalian brain and shown to consist of two classes of subunit, a larger (approximately 78,000 M(r)) protein (alpha) whose N-terminal sequence is identical to that of a cloned, alpha-DTX-sensitive K+ channel, and a...

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Bibliographic Details
Published in:Biochemistry (Easton) 1992-11, Vol.31 (45), p.11084-11088
Main Authors: Parcej, David N, Scott, Victoria E. S, Dolly, J. Oliver
Format: Article
Language:English
Subjects:
Animals
Biological and medical sciences
Brain - metabolism
Cattle
Cell physiology
Chromatography, Gel
Elapid Venoms - pharmacology
Electrophoresis, Polyacrylamide Gel
Fundamental and applied biological sciences. Psychology
Membrane and intracellular transports
Molecular and cellular biology
Neurotoxins - pharmacology
Potassium Channels - chemistry
Potassium Channels - drug effects
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Summary:Neuronal acceptors for alpha-dendrotoxin (alpha-DTX) have recently been purified from mammalian brain and shown to consist of two classes of subunit, a larger (approximately 78,000 M(r)) protein (alpha) whose N-terminal sequence is identical to that of a cloned, alpha-DTX-sensitive K+ channel, and a novel M(r) 39,000 (beta) polypeptide of unknown function. However, little information is available regarding the oligomeric composition of these native molecules. By sedimentation analysis of alpha-DTX acceptors isolated from bovine cortex, two species have been identified. A minority of these oligomers contain only the larger protein, while the vast majority possess both subunits. Based on accurate determination of the molecular weights of these two forms it is proposed that alpha-DTX-sensitive K+ channels exist as alpha 4 beta 4 complexes because this combination gives the best fit to the experimental data.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00160a018