Abstract
A protein, identifiable as calmodulin (CaM), has been isolated from the seedling tissue of Pharbitis nil. The method has been developed to isolate a high quality protein from plant tissue containing the high content of polyphenols. This protein was relatively heat-stable and bound to hydrophobic resin in calcium-dependent manner. It was recognized by the antibody against pea and carrot, but did not bind to antibody against Dictyostelium discoideum. This protein had Mr of 15 kDa and 18.5 kDa in the presence and absence of Ca2+, respectively, and was able to stimulate calmodulin-deficient cAMP phosphodiesterase. Based on its migration on SDS-PAGE gels, Mr and binding to anti-CaM antibodies it was deduced that calmodulin from P. nil is essentially identical to calmodulin isolated from other plants.
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Jaworski, K., Szmidt-Jaworska, A., Tretyn, A. et al. Calmodulin from Pharbitis nil: Purification and Characterization. Biologia Plantarum 48, 55–60 (2004). https://doi.org/10.1023/B:BIOP.0000024275.66196.d9
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DOI: https://doi.org/10.1023/B:BIOP.0000024275.66196.d9