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PMID: 2446925 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

The N-terminal half of the heavy chain of botulinum type A neurotoxin forms channels in planar phospholipid bilayers.

FEBS letters ·Vol. 226 ·No. 1 ·1987-12-21 ·Pages 115-20

Blaustein RO, Germann WJ, Finkelstein A, DasGupta BR

Abstract

The heavy chain of botulinum type A neurotoxin forms channels in planar phospholipid bilayer membranes. Channel activity is confined to the N-terminal half of this chain; the C-terminal half is inactive. Channel activity is stimulated by low pH (4.5-5.5) on the cis side (the side to which protein is added), neutral pH on the opposite (trans) side, and cis positive voltages. These findings are strikingly similar to those previously reported for analogous fragments of diphtheria and tetanus toxins.

MeSH Terms
Botulinum Toxins Hydrogen-Ion Concentration Ion Channels/physiology Lipid Bilayers Macromolecular Substances Models, Biological Molecular Weight Neurotoxins Phosphatidylcholines Phosphatidylethanolamines Phosphatidylserines
Chemicals
Ion Channels Lipid Bilayers Macromolecular Substances Neurotoxins Phosphatidylcholines Phosphatidylethanolamines Phosphatidylserines Botulinum Toxins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Blaustein R O
Department of Physiology, Albert Einstein College of Medicine, Bronx, NY 10461.
Germann W J
Finkelstein A
DasGupta B R
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1987-12-21
Pages
115-20
Language
English
Region
England
NLM ID
0155157
Subset
IM
Grants
NIGMS NIH HHS · GM29210-10 · United States
NINDS NIH HHS · NS17742 · United States
NINDS NIH HHS · NS24545 · United States
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