Interactions of saccharides with concanavalin A. Relation between calcium ions and the binding of saccharides to concanavalin A

C. F. Brewer, D. M. Marcus, A. P. Grollman, H. Sternlicht

Research output: Contribution to journalArticle

24 Scopus citations

Abstract

Previous studies were interpreted as showing that transition metal and calcium ions must be bound to concanavalin A before this lectin can bind sugars. In contrast, it was found that the addition of calcium ions fails to affect the following properties of manganese concanavalin A if the metalloprotein is prepared in their presence: electron spin resonance spectrum of the manganese ion in the protein; spin lattice relaxation time of solvent water protons measured in the presence of the protein; and spin lattice and transverse relaxation times of the 13C carbons of α methyl D glucopyranoside (uniformly enriched with 14% 13C) in the presence of manganese concanavalin A. These results indicate that saccharide binding activity of the protein is independent of calcium ion binding if a transition metal ion (Mn2+) initially binds to the protein in the presence of calcium ions. The role of calcium ion binding to concanavalin A appears to be that of accelerating the rate of formation of the final transition metal protein complex.

Original languageEnglish (US)
Pages (from-to)4614-4616
Number of pages3
JournalJournal of Biological Chemistry
Volume249
Issue number14
StatePublished - Dec 1 1974

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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