Macromolecular characterization of muscle membranes. Acetylcholine receptor of normal and denervated muscle

C. G. Andrew, R. R. Almon, S. H. Appel

Research output: Contribution to journalArticle

18 Scopus citations

Abstract

Two major membrane fractions isolated from denervated and control rat muscle have been assessed in vitro for their ability to bind α bungarotoxin, an elapid neurotoxin specific for the acetylcholine receptor. Membranes isolated from the initial nuclear pellet (fraction I) bound 1.04 pmoles of 125I α bungarotoxin per mg, while membranes isolated from the postmitochondrial supernatant (Fraction II) bound 0.27 pmole per mg. The toxin binding was blocked by several cholinergic inhibitors. Following subfractionation of the two major muscle membrane fractions, the α bungarotoxin binding was preferentially localized to subfractions enriched in two surface membrane markers: sodium, potassium stimulated, magnesium dependent adenosine triphosphatase, and sialic acid containing macromolecules. Following muscle denervation for 10 days the toxin binding increased to 16.87 pmoles per mg (Fraction I) and 5.38 pmoles per mg (Fraction II). The data suggest that 125I α bungarotoxin binding may serve as an additional surface membrane marker of considerable importance in assessment of the subcellular site of origin of isolated muscle membranes.

Original languageEnglish (US)
Pages (from-to)6163-6165
Number of pages3
JournalJournal of Biological Chemistry
Volume249
Issue number19
StatePublished - 1974

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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