The binding of calcium ions to hemocyanin from Levantina hierosolima at physiological pH

Alexander Klarman*, Nurith Shaklai, Ezra Daniel

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

The binding of Ca2+ to Levantina hierosolima hemocyanin at physiological pH, 8.2, was studied. 20 moles of binding sites per unit of 50 000 g protein were found. In parallel, the effect of Ca2+ on the aggregation state of the macromolecules was examined. The correlation between the binding of Ca2+ and the association behavior is explained by the formation of calcium chelates involving carboxylate and imidazole side chains of the proteins.

Original languageEnglish
Pages (from-to)150-157
Number of pages8
JournalBBA - Protein Structure
Volume257
Issue number1
DOIs
StatePublished - 26 Jan 1972

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