Effect of α-Bungarotoxin on Acetylcholinesterase bound to Mouse Diaphragm Endplates
IT has been shown that α-bungarotoxin (α-Bgt) irreversibly blocks cholinoreceptors 1–10 , and that D -(+)tubocurarine (TC) protects these receptors from the toxin 4–7 . On the other hand, it has been emphasized that α-Bgt has no effect on the catalytic activity of acetylcholinesterase (AChE) 4,6,9 ,...
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Veröffentlicht in: | Nature. New biology (London) 1972-09, Vol.239 (90), p.91-92 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | IT has been shown that α-bungarotoxin (α-Bgt) irreversibly blocks cholinoreceptors
1–10
, and that
D
-(+)tubocurarine (TC) protects these receptors from the toxin
4–7
. On the other hand, it has been emphasized that α-Bgt has no effect on the catalytic activity of acetylcholinesterase (AChE)
4,6,9
, and it was concluded that the cholinoreceptor and AChE must be two different macromolecules
8,9
. Because typical cholinolytics, including TC and gallamine, characteristically influence the kinetics of a membrane-bound AChE
11,12
, it seemed justified to reinvestigate whether α-Bgt really is an exception in this respect. |
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ISSN: | 0090-0028 2058-1092 |
DOI: | 10.1038/newbio239091a0 |