Calcium binding to calmodulin. cooperativity of the calcium-binding sites

Shozo Iida, James D. Potter

Research output: Contribution to journalArticle

44 Scopus citations

Abstract

The effects of Mg2+ ion, pH, and KCl concentration on Ca2+ binding to calmodulin were studied by using a Ca2+ ion-sensitive electrode. The Ca2+ ion affinity of calmodulin increased with increasing pH or decreasing KCl concentration. Cooperativity between the Ca2+ sites was observed, and increased with decreasing pH or increasing KCl concentration. Free Ca2+ ion concentration was decreased by adding MgCl2 ion at low Mg2+ concentration and increased at higher concentrations in the presence of small amounts of Ca2+ ion. The decrease of free Ca2+ ion concentration by Mg2+ ion strongly suggests cooperativity between the Ca2+-binding sites, and it is difficult to explain the decrease in terms of the ordered binding models previously proposed. These results can be explained by a simple model which has four equivalent binding sites that bind Ca2+ and Mg2+ competitively, and showing cooperativity when either Ca2+ or Mg2+ is bound. Mg2+ ion binding to calmodulin was measured in the presence or absence of Ca2+ to confirm the validity of this model, and no Mg2+-specific site was observed.

Original languageEnglish (US)
Pages (from-to)1765-1772
Number of pages8
JournalJournal of Biochemistry
Volume99
Issue number6
DOIs
StatePublished - Jan 1 1986

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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