Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Plant Physiology 68:377-381 (1981)
© 1981 American Society of Plant Biologists

This Article
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 CrossRef
Right arrow Citing Articles via Web of Science (38)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Cocucci, M.
Right arrow Articles by Ballarin-Denti, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Cocucci, M.
Right arrow Articles by Ballarin-Denti, A.
Agricola
Right arrow Articles by Cocucci, M.
Right arrow Articles by Ballarin-Denti, A.
Articles

Effect of Polar Lipids on ATPase Activity of Membrane Preparations from Germinating Radish Seeds 1

Maurizio Cocucci and Antonio Ballarin-Denti

Centro di Studio del Consiglio Nazionale delle Ricerche per la Biologia Cellulare e Molecolare delle Piante, c/o Istituto di Scienze Botaniche, Università di Milano, 20133 Milano, Italy

Membrane preparation (sedimenting between 13,000g and 80,000g) of germinating radish seeds (Raphanus sativus L.) was active in hydrolyzing ATP and, to a lesser extent, a variety of other phosphorylated compounds. Dicyclohexylcarbodiimide (DCCD) and diethylstilbestrol significantly inhibited the ATPase activity (40%) while their effect on hydrolysis of other phosphorylated compounds was much less.

The sucrose density gradient analysis of the membrane preparation showed that the position of the DCCD-sensitive K+-dependent ATPase was similar to that found for plasma membrane of other plant material.

Cholate treatment of membrane preparation removes almost all phospholipids, and ATPase activity is barely detectable. However, the addition of polar lipids completely restores the ATPase activity but does not restore general phosphatase activity.

The ATPase of the polar lipids restored cholate preparation, showed a high sensitivity to DCCD and diethylstilbestrol (up to 90% inhibition), a complete dependence on Mg2+, and a strong dependence on K+ at low concentration; the pH optimum of ATPase was close to 6.5, and the Km for ATP-Mg was 0.51 millimolar. ATPase activity was much greater when polar lipids from 24-hour-germinated seeds were added.


1 This work is part of a research program of Consiglio Nazionale delle Ricerche on the biology of reproduction.







HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1981 by the American Society of Plant Biologists