Plant Physiol. Illumina
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Web of Science (25)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Tassoni, A.
Right arrow Articles by Bagni, N.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Tassoni, A.
Right arrow Articles by Bagni, N.
Agricola
Right arrow Articles by Tassoni, A.
Right arrow Articles by Bagni, N.

Characterization of Spermidine Binding to Solubilized Plasma Membrane Proteins from Zucchini Hypocotyls1

Annalisa Tassoni, Fabiana Antognoni, Maria Luisa Battistini, Olivier Sanvido, and Nello Bagni*

Dipartimento di Biologia Evoluzionistica Sperimentale, Università di Bologna, Via Irnerio 42, 40126 Bologna, Italy

In this work [14C]spermidine binding to total proteins solubilized from plasma membrane purified from zucchini (Cucurbita pepo L.) hypocotyls was investigated. Proteins were solubilized using octyl glucoside as a detergent. Specific polyamine binding was thermolabile, reversible, pH dependent with an optimum at pH 8.0, and had a Kd value of 5 µM, as determined by glass-fiber-filter assays. Sephadex G-25 M gel-filtration assays confirmed the presence of a spermidine-protein(s) complex with a specific binding activity. By sodium dodecyl sulfate-polyacrylamide gel electrophoresis and native polyacrylamide gel electrophoresis of collected fractions having the highest specific spermidine-binding activity, several protein bands (113, 75, 66, and 44 kD) were identified. The specificity of spermidine binding was examined by gel-filtration competition experiments performed using other polyamines and compounds structurally related to spermidine. Partial purification on Sephadex G-200 led to the identification of 66- and 44-kD protein bands, which may represent the putative spermidine-binding protein(s) on the plasmalemma.

1   This work was supported in part by funds from the National Research Council of Italy, special project Ricerche Avanzate per Innovazioni nel Sistema Agricolo, subproject no. 2, and in part by funds from the Ministero dell'Università, della Ricerca Scientifica e Tecnologica. O.S. was a recipient of a grant from the Roche Research Foundation (Basel, Switzerland).
*   Corresponding author; e-mail bagninel{at}kaiser.alma.unibo.it; fax 39-51-242576.

Plant Physiol. (1998) 117: 971-977
Copyright Clearance Center:   0032-0889/98/117/0971/07
© 1998 American Society of Plant Physiologists




This article has been cited by other articles:


Home page
 Plant Physiol.Home page
F. Zhao, C.-P. Song, J. He, and H. Zhu
Polyamines Improve K+/Na+ Homeostasis in Barley Seedlings by Regulating Root Ion Channel Activities
Plant Physiology, November 1, 2007; 145(3): 1061 - 1072.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
A. Tassoni, R. M. Napier, M. Franceschetti, M. A. Venis, and N. Bagni
Spermidine-Binding Proteins. Purification and Expression Analysis in Maize
Plant Physiology, April 1, 2002; 128(4): 1303 - 1312.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1998 by the American Society of Plant Biologists