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Updated: Jun 22, 2026

Pull-down of Calmodulin-binding Proteins
Published on: January 23, 2012
The activation of chick alkaline phosphatase by calmodulin
L Sivanaesan1, T K Kwan, R Perumal
1Department of Biochemistry, Faculty of Medicine, University of Malaya, Kuala Lumpur.
Abstract:
Calmodulin, an activator protein in most calcium-dependent processes, was isolated to apparent homogeneity from the femurs of 1-day old chicks using phenyl-Sepharose and high performance liquid chromatography. The purified calmodulin was found to produce a 6-fold increase in the activity of alkaline phosphatase isolated from the same source. A Ca2+ concentration of 10(-5) M was required for the activation. Purification of alkaline phosphatase involved acetone precipitation, DEAE-Sephacel and Sephadex G-200 column chromatography. The enzyme was purified to 540-fold and had a specific activity of 10.75 U/mg protein.
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