Calreticulin Is the Major Ca 2+ Storage Protein in the Endoplasmic Reticulum of the Pea Plant ( Pisum sativum )

Calreticulin Is the Major Ca 2+ Storage Protein in the Endoplasmic Reticulum of the Pea Plant (... A 56kDa protein with high similarity in its N-terminal amino acid sequence to animal calreticulin and 100% homology with the N-terminal amino acids of spinach calreticulin has been identified in seeds of the pea plant ( Pisum sativum ). A new purification procedure is described by which the calreticulin-like protein was selectively solubilized by incubation with deoxycholate and HgCl 2 from microsomes enriched for endoplasmic reticulum. Following Mono Q ion exchange chromatography of the deoxycholate extract by fast protein liquid chromatography, the calreticulin-like protein was obtained in nearly pure form. This purified protein is similar to animal calreticulin in apparent mass, characteristic blue staining with Stains-all dye and calcium-binding ability. In addition, this protein is recognized only by affinity purified antibodies against rabbit calreticulin and is not recognized by anti-calsequestrin antibodies. Our data suggested that calreticulin rather than calsequestrin functions as the Ca 2+ -storage protein in the endoplasmic reticulum of pea plants. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biochemical and Biophysical Research Communications Elsevier

Calreticulin Is the Major Ca 2+ Storage Protein in the Endoplasmic Reticulum of the Pea Plant ( Pisum sativum )

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Publisher
Elsevier
Copyright
Copyright © 1995 Academic Press
ISSN
0006-291x
D.O.I.
10.1006/bbrc.1995.1777
Publisher site
See Article on Publisher Site

Abstract

A 56kDa protein with high similarity in its N-terminal amino acid sequence to animal calreticulin and 100% homology with the N-terminal amino acids of spinach calreticulin has been identified in seeds of the pea plant ( Pisum sativum ). A new purification procedure is described by which the calreticulin-like protein was selectively solubilized by incubation with deoxycholate and HgCl 2 from microsomes enriched for endoplasmic reticulum. Following Mono Q ion exchange chromatography of the deoxycholate extract by fast protein liquid chromatography, the calreticulin-like protein was obtained in nearly pure form. This purified protein is similar to animal calreticulin in apparent mass, characteristic blue staining with Stains-all dye and calcium-binding ability. In addition, this protein is recognized only by affinity purified antibodies against rabbit calreticulin and is not recognized by anti-calsequestrin antibodies. Our data suggested that calreticulin rather than calsequestrin functions as the Ca 2+ -storage protein in the endoplasmic reticulum of pea plants.

Journal

Biochemical and Biophysical Research CommunicationsElsevier

Published: Jun 6, 1995

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