Interactions of erythrosin B (U.S. F, D & C Red 3) with rat cortical membranes

E. K. Silbergeld, S. M. Anderson, S. J. Morris

Research output: Contribution to journalArticlepeer-review

Abstract

Erythrosin B inhibits Na, K-ATPase in rat brain tissue as demonstrated by studying glycoside binding, ATPase activity and ion fluxes. The potency of the noncompetitive inhibition of [3H]-ouabain binding by erythrosin B is influenced by glycoside concentration, monovalent cation concentration, and incubation time. [14C]- Erythrosin B binds to synaptic membranes prepared from rat cortex. Erythrosin B and some of its structural analogs inhibit both [3H]-ouabain and [14C]-erythrosin B binding, but ouabain and other glycosides do not inhibit the binding of [14C]-erythrosin B. Subcellular distributions of [3H]-ouabain and [14C]- erythrosin B binding in fractionated cortical tissue preparations are equivalent and parallel ATPase activity. The dissimilar response of [3H]-ouabain binding and [14C]-erythrosin B binding to changes in tissue preparation, incubation temperature, and partial solubilization of binding sites by deoxycholate (DOC) Suggests two separate binding sites for erythrosin and ouabain to rat cortical membranes.

Original languageEnglish (US)
Pages (from-to)957-969
Number of pages13
JournalLife Sciences
Volume31
Issue number10
DOIs
StatePublished - Sep 6 1982
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Pharmacology, Toxicology and Pharmaceutics(all)

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