Fate of alpha-bungarotoxin bound to acetylcholine receptors of normal and denervated muscle.

Science (New York, N.Y.) ·Vol. 184 ·No. 4135 ·1974-04-26 ·Pages 473-5

Berg DK, Hall ZW

Abstract

In organ culture, alpha-[(125)I]bungarotoxin bound to extrajunctional receptors of denervated muscle is lost from the tissue at a more rapid rate than the toxin bound to the junctional receptors of normal muscle. The rapid loss of toxin from denervated muscle can be blocked by inhibitors of energy production and protein synthesis, and may reflect turnover of the toxin-receptor complex in the membrane.

MeSH Terms

Animals Binding Sites Bungarotoxins/metabolism Cycloheximide/pharmacology Diaphragm Iodine Radioisotopes Kinetics Muscle Denervation Muscle Proteins/biosynthesis Muscles/innervation,metabolism Neuromuscular Junction/metabolism Organ Culture Techniques Puromycin/pharmacology Rats Receptors, Cholinergic/drug effects

Chemicals

Bungarotoxins Iodine Radioisotopes Muscle Proteins Receptors, Cholinergic Puromycin Cycloheximide

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Berg D K

Hall Z W

Article Info

Journal

Science (New York, N.Y.)

Abbr.

Science

ISSN

0036-8075

DOI

10.1126/science.184.4135.473

Published

1974-04-26

Pages

473-5

Language

English

Region

United States

NLM ID

0404511

Subset

External Links

PubMed source DOI: 10.1126/science.184.4135.473 View journal details

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Fate of alpha-bungarotoxin bound to acetylcholine receptors of normal and denervated muscle.

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