Related Experiment Video
Updated: Aug 8, 2026

Pull-down of Calmodulin-binding Proteins
Published on: January 23, 2012
Characterization of oat calmodulin and radioimmunoassay of its subcellular distribution
1Department of Botany, The University of Texas at Austin, Austin, Texas 78712.
Abstract:
A protein identifiable as calmodulin has been isolated from oat (Avena sativa, var Garry) tissues. This protein is relatively heat stable, binds to hydrophobic gels, and phenothiazines in a calcium-dependent fashion, and binds to antibody to rat testes calmodulin. Based on its migration on sodium dodecyl sulfate-polyacrylamide gels, ultraviolet absorption spectrum, and amino acid composition, oat calmodulin is essentially identical to calmodulin isolated from other higher plants. Radioimmunoassays indicate that calmodulin is associated with isolated oat protoplasts, mitochondria, etioplasts, and nuclei and also appears to be a component of oat cell wall fractions.
More Related Videos
13:40Live Cell Calcium Imaging Combined with siRNA Mediated Gene Silencing Identifies Ca2+ Leak Channels in the ER Membrane and their Regulatory Mechanisms
Published on: July 7, 2011
10:16Autoradiography as a Simple and Powerful Method for Visualization and Characterization of Pharmacological Targets
Published on: March 12, 2019