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Updated: May 5, 2026

Pull-down of Calmodulin-binding Proteins
Published on: January 23, 2012
Calcium-binding and its effect on circular dichroism of plant calmodulin
1Biochemical Institute, University of Freiburg, Hermann Herder Straße 7, D-7800, Freiburg, Federal Republic of Germany.
Abstract:
The Ca(2+)-binding properties of calmodulin purified from zucchini (Cucurbita pepo L.) has been determined. A value of 3.3 mol Ca(2+) per mol of zucchini calmodulin was measured at pH 7.5 by equilibrium chromatography. The far-and near-UV circular-dichroic spectra of the Ca(2+)-and Mg(2+)-saturated as well as from the metal-free forms of zucchini calmodulin reveal that upon Ca(2+)-binding the α-helix content increases. A comparison with the spectra of vertebrate calmodulin indicates that both calmodulin have a similar secondary structure, similar Ca(2+)-induced conformational changes and the same number of Ca(2+)-binding sites.
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