Purification of the Plasma Membrane Ca2+-ATPase from Radish Seedlings by Calmodulin-Agarose Affinity Chromatography1-Reference-Cited by-同舟云学术

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

Published:1998-02-01 Issue:2 Volume:116 Page:845-851
ISSN:1532-2548
Container-title:Plant Physiology
language:en
Short-container-title:

Author:

Bonza Cristina¹,Carnelli Antonella¹,De Michelis Maria Ida²,Rasi-Caldogno Franca¹

Affiliation:

1. Dipartimento di Biologia L. Gorini, Università di Milano, via G. Celoria 26, 20133 Milano, Italy (C.B., A.C., F.R.-C.)

2. Istituto Botanico Hanbury ed Orto Botanico dell'Università, corso Dogali 1, 16136 Genova, Italy (M.I.D.M.)

Abstract

Abstract 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 withn-dodecyl β-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 thalianachloroplast envelope.

Publisher

Oxford University Press (OUP)

Subject

Plant Science,Genetics,Physiology

Link

http://academic.oup.com/plphys/article-pdf/116/2/845/37209153/plphys_v116_2_845.pdf

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