Alpha-toxin binding to acetylcholine receptor alpha 179-191 peptides: intrinsic fluorescence studies

Interactions between two alpha-toxins and the synthetic peptides alpha 179-191 from both calf and human acetylcholine receptor alpha-subunit sequences have been studied by measurements of quenching of intrinsic fluorescence after toxin addition. Dissociation constants of approx. 5 x 10(-8) M for bin...

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Bibliographic Details
Published in:FEBS letters 1988-04, Vol.231 (1), p.212
Main Authors: Radding, W, Corfield, P W, Levinson, L S, Hashim, G A, Low, B W
Format: Article
Language:English
Subjects:
Animals
Cattle
Cobra Neurotoxin Proteins - metabolism
Cytochrome d Group
Cytochromes - metabolism
Elapid Venoms - metabolism
Electron Transport Complex IV - metabolism
Erabutoxins - metabolism
Humans
Macromolecular Substances
Protein Binding
Receptors, Cholinergic - metabolism
Spectrometry, Fluorescence
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Summary:Interactions between two alpha-toxins and the synthetic peptides alpha 179-191 from both calf and human acetylcholine receptor alpha-subunit sequences have been studied by measurements of quenching of intrinsic fluorescence after toxin addition. Dissociation constants of approx. 5 x 10(-8) M for binding of calf peptide by both alpha-cobratoxin and erabutoxin a have been estimated. The binding of alpha-cobratoxin to calf peptide, which leads to marked quenching of fluorescence intensity, is inhibited by a 10(4) molar excess of acetylcholine. The human alpha 179-191 peptide binds to alpha-cobratoxin, but not, under comparable conditions, to erabutoxin a.
ISSN:0014-5793
DOI:10.1016/0014-5793(88)80733-6