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. 1984 Jun;75(2):382–386. doi: 10.1104/pp.75.2.382

Characterization of Oat Calmodulin and Radioimmunoassay of Its Subcellular Distribution 1

Ronald L Biro 1,2,2, Sun Daye 1,2,3, Bruce S Serlin 1,2, Maurice E Terry 1,2, Neeraj Datta 1,2, Sudhir K Sopory 1,2,4, Stanley J Roux 1,2
PMCID: PMC1066917  PMID: 16663631

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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