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


     

Plant Physiology 65:314-318 (1980)
© 1980 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 HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Web of Science (17)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Rapp, B. J.
Right arrow Articles by Randall, D. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Rapp, B. J.
Right arrow Articles by Randall, D. D.
Agricola
Right arrow Articles by Rapp, B. J.
Right arrow Articles by Randall, D. D.
Articles

Pyruvate Dehydrogenase Complex from Germinating Castor Bean Endosperm 1

Barbara J. Rapp and Douglas D. Randall2

Department of Biochemistry, University of Missouri, Columbia, Missouri 65211

Subcellular organelles from castor bean (Ricinus communis) endosperm were isolated on discontinuous sucrose gradients from germinating seeds which were 1 to 7 days postimbibition. Marker enzyme activities of the organelles were measured (fumarase, catalase, and triose phosphate isomerase) and the homogeneity of the organelle fractions was examined by electron microscopy. Pyruvate dehydrogenase complex activity was measured only in the mitochondrial fraction and attempts to activate or release the enzyme from the proplastid were not successful. A pathway is proposed for the most efficient use of endosperm carbon for de novo fatty acid biosynthesis that does not require the presence of the pyruvate dehydrogenase complex in the proplastid to provide acetyl-coenzymeA.

2 To whom requests for reprints may be addressed.

1 This work was supported by National Science Foundation Grant PCM 77-11390 and Missouri Agricultural Experiment Station, Series No. 8374.




This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
Y. Guan, S. Rawsthorne, G. Scofield, P. Shaw, and J. Doonan
Cloning and Characterization of a Dihydrolipoamide Acetyltransferase (E2) Subunit of the Pyruvate Dehydrogenase Complex from Arabidopsis thaliana
J. Biol. Chem., March 10, 1995; 270(10): 5412 - 5417.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1980 by the American Society of Plant Biologists