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

Alexander Klarman; Nurith Shaklai; Ezra Daniel

doi:10.1016/0005-2795(72)90264-4

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 journal › Article › peer-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 language	English
Pages (from-to)	150-157
Number of pages	8
Journal	BBA - Protein Structure
Volume	257
Issue number	1
DOIs	https://doi.org/10.1016/0005-2795(72)90264-4
State	Published - 26 Jan 1972

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title = "The binding of calcium ions to hemocyanin from Levantina hierosolima at physiological pH",

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.",

author = "Alexander Klarman and Nurith Shaklai and Ezra Daniel",

year = "1972",

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doi = "10.1016/0005-2795(72)90264-4",

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T1 - The binding of calcium ions to hemocyanin from Levantina hierosolima at physiological pH

AU - Klarman, Alexander

AU - Shaklai, Nurith

AU - Daniel, Ezra

PY - 1972/1/26

Y1 - 1972/1/26

N2 - 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.

AB - 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.

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U2 - 10.1016/0005-2795(72)90264-4

DO - 10.1016/0005-2795(72)90264-4

M3 - מאמר

AN - SCOPUS:0015524296

VL - 257

SP - 150

EP - 157

JO - Biochimica et Biophysica Acta - Proteins and Proteomics

JF - Biochimica et Biophysica Acta - Proteins and Proteomics

SN - 1570-9639

IS - 1

ER -

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

Abstract

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