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Plant Physiology 75:382-386 (1984)
© 1984 American Society of Plant Biologists

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Articles

Characterization of Oat Calmodulin and Radioimmunoassay of Its Subcellular Distribution 1

Ronald L. Biro2, Sun Daye3, Bruce S. Serlin, Maurice E. Terry, Neeraj Datta, Sudhir K. Sopory4 and Stanley J. Roux

Department of Botany, The University of Texas at Austin, Austin, Texas 78712, Department of Plant Pathology and Crop Physiology, Louisiana State University Agricultural Experiment Station, Baton Rouge Louisiana 70803

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.

2 Wake Forest University, Biology Department, Winston-Salem, North Carolina 27901.

3 Hopei Teachers University, Biology Department, Peoples' Republic of China.

4 Jawaharlal Nehru University, School of Life Sciences, New Delhi 110067, India.

1 Supported by grants from the National Aeronautics and Space Administration (NSG 7480), The National Science Foundation (PCM 81-03429), and The Robert A. Welch Foundation (F 858) to S. J. R.




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