Binding sites for [3H]-acetylcholine and 125I-α-bungarotoxin in the optic ganglion of Loligo pealii

Shu-jen Chen, Rita Spathis, Jakob Schmidt

Research output: Contribution to journalArticle

10 Scopus citations

Abstract

1. 1. In the optic ganglion of Loligo pealii, binding sites for [3H]-acetylcholine (KD: 5.2 × 10-7 M; Bmax: 1.7 × 10-11 mol/g tissue) and 125I-α-bungarotoxin (KD: 3.3 × 10-9 M; Bmax: 9.7 × 10-11 mol/g tissue) were observed. 2. 2. Both sites are blocked by nicotinic compounds, but differ significantly in their affinity for individual ligands, with the acetylcholine site preferentially binding agonists, and the toxin site, antagonists. 3. 3. The acetylcholine site is substantially more thermolabile than the toxin site. 4. 4. A partial separation of the two binding activities is accomplished by sucrose density centrifugation. 5. 5. These observations and a comparison with other tissues (Torpedo californica electroplaque; chick optic lobe; rat brain) suggest the presence, in the squid, of more than one kind of neuronal nicotinic receptor.

Original languageEnglish (US)
Pages (from-to)317-323
Number of pages7
JournalComparative Biochemistry and Physiology. Part C, Comparative
Volume90
Issue number2
DOIs
StatePublished - 1988

All Science Journal Classification (ASJC) codes

  • Immunology
  • Pharmacology

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