Characterization of Oat Calmodulin and Radioimmunoassay of Its Subcellular Distribution | Zendy

R. L. Biro | Zendy; Sun Daye | Zendy; Bruce S. Serlin | Zendy; Maurice E. Terry | Zendy; Neeraj Datta | Zendy; Sudhir K. Sopory | Zendy; Stanley J. Roux | Zendy

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Characterization of Oat Calmodulin and Radioimmunoassay of Its Subcellular Distribution

Author(s) -

R. L. Biro,

Sun Daye,

Bruce S. Serlin,

Maurice E. Terry,

Neeraj Datta,

Sudhir K. Sopory,

Stanley J. Roux

Publication year - 1984

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.75.2.382

Subject(s) - calmodulin , avena , radioimmunoassay , biochemistry , calcium , chemistry , sodium , sodium dodecyl sulfate , polyacrylamide gel electrophoresis , biology , enzyme , botany , organic chemistry

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.

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