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Purification of the Plasma Membrane Ca2+-ATPase from Radish Seedlings by Calmodulin-Agarose Affinity Chromatography1

Cristina Bonza*, Antonella Carnelli, Maria Ida De Michelis2, and Franca Rasi-Caldogno3

Dipartimento di Biologia L. Gorini, Università di Milano, via G. Celoria 26, 20133 Milano, Italy (C.B., A.C., F.R.-C.); and Istituto Botanico Hanbury ed Orto Botanico dell'Università, corso Dogali 1, 16136 Genova, Italy (M.I.D.M.)

The Ca2+-ATPase of the plasma membrane (PM) of germinating radish (Raphanus sativus L.) seeds was purified by calmodulin (CaM)-affinity chromatography using a batch procedure. PM purified by aqueous two-phase partitioning was solubilized with n-dodecyl beta -d-maltoside and applied to a CaM-agarose matrix. After various washings with decreasing Ca2+ concentrations, the Ca2+-ATPase was eluted with 5 mm ethylenediaminetetraacetate (EDTA). The EDTA-eluted fraction contained about 25% of the loaded Ca2+-ATPase activity, with a specific activity 70-fold higher than that of the starting PM fraction. The EDTA-eluted fraction was highly enriched in a 133-kD polypeptide, which was identified as the PM Ca2+-ATPase by 125I-CaM overlay and fluorescein-isothiocyanate labeling. The PM Ca2+-ATPase cross-reacted with an antiserum against a putative Ca2+-ATPase of the Arabidopsis thaliana chloroplast envelope.

1   This work was supported by a grant from the Italian Ministry for University and Scientific and Technologic Research (40% quote).
2   Present address: Dipartimento di Biologia "L. Gorini," Università di Milano, via G. Celoria 26, 20133 Milano, Italy.
3   Franca Rasi-Caldogno, who played a pivotal role in this work, prematurely died before its completion.
*   Corresponding author; e-mail fimca{at}imiucca.unimi.it; fax 39-2-26-60-4399.

Plant Physiol. (1998) 116: 845-851
Copyright Clearance Center:   0032-0889/98/116/0845/07
© 1998 American Society of Plant Physiologists




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