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


     


Plant Physiology 72:134-138 (1983)
© 1983 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 (26)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Davies, D. D.
Right arrow Articles by Asker, H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Davies, D. D.
Right arrow Articles by Asker, H.
Agricola
Right arrow Articles by Davies, D. D.
Right arrow Articles by Asker, H.
Articles

Synthesis of Oxalic Acid by Enzymes from Lettuce Leaves

David D. Davies1 and Hassan Asker1

Station de Physiologie Végétale, Institut National de la Recherche Agronomique, La Grande Ferrade, 33140 Pont-de-la-Maye, Bordeaux, France

A rapid purification of lactate dehydrogenase and glycolate oxidase from lettuce (Lactuca sativa) leaves is described. The kinetics of both enzymes are reported in relation to their possible roles in the production of oxalate. Lettuce lactate dehydrogenase behaves like mammalian dehydrogenase, catalyzing the dismutation of glyoxylate to glycolate and oxalate. A model is proposed in which glycolate oxidase in the peroxisomes and lactate dehydrogenase in the cytosol are involved in the production of oxalate. The effect of pH on the balance between oxalate and glycolate produced from glyoxylate suggests that in leaves lactate dehydrogenase may function as part of an oxalate-based biochemical, pH-stat.


1 Present address: School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ U.K.




This article has been cited by other articles:


Home page
J Exp BotHome page
H.-W. Xu, X.-M. Ji, Z.-H. He, W.-P. Shi, G.-H. Zhu, J.-K. Niu, B.-S. Li, and X.-X. Peng
Oxalate accumulation and regulation is independent of glycolate oxidase in rice leaves
J. Exp. Bot., June 1, 2006; 57(9): 1899 - 1908.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1983 by the American Society of Plant Biologists