Characterization of Oat Calmodulin and Radioimmunoassay of Its Subcellular Distribution 1

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...

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Bibliographic Details
Published in:	Plant physiology (Bethesda) 1984-06, Vol.75 (2), p.382-386
Main Authors:	Biro, Ronald L., Daye, Sun, Serlin, Bruce S., Terry, Maurice E., Datta, Neeraj, Sopory, Sudhir K., Roux, Stanley J.
Format:	Article
Language:	eng
Online Access:	Get full text
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Summary:	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.
ISSN:	0032-0889 1532-2548