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


     


Plant Physiology 70:1582-1585 (1982)
© 1982 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 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 Google Scholar
Google Scholar
Right arrow Articles by Hampp, R.
Right arrow Articles by Tarczynski, M. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hampp, R.
Right arrow Articles by Tarczynski, M. C.
Agricola
Right arrow Articles by Hampp, R.
Right arrow Articles by Tarczynski, M. C.
Articles

Profile of Basic Carbon Pathways in Guard Cells and Other Leaf Cells of Vicia faba L. 1

Rüdiger Hampp2, William H. Outlaw, Jr. and Mitchell C. Tarczynski

Department of Biological Science (Unit I), Florida State University, Tallahassee, Florida 32306

Guard cells and three other cell types from Vicia faba L. `Longpod' leaflets were assayed for enzymes that catalyze one step in each of five major carbon pathways in green plants: the photosynthetic carbon reduction pathway (ribulose-bisphosphate carboxylase, EC 4.1.1.39), the photosynthetic carbon oxidation pathway (hydroxypyruvate reductase, EC 1.1.1.81), glycolysis ([NAD] glyceraldehyde-P dehydrogenase, EC 1.2.1.12), the oxidative pentose-P pathway (6-P-gluconate dehydrogenase, EC 1.1.1.44), and the tricarboxylic acid pathway (fumarase, EC 4.2.1.2). Neither ribulose-bisphosphate carboxylase nor hydroxypyruvate reductase could be detected in guard cells or epidermal cells; high levels of these activities were present in mesophyll cells. The specific activity of fumarase (protein basis) was about 4-fold higher in guard cells than in epidermal, palisade parenchyma or spongy parenchyma cells. (NAD) glyceraldehyde-P and 6-P-gluconate dehydrogenases also were present at high protein specific activities in guard cells (2- to 4-fold that in meosphyll cells).

It was concluded that the capacity for metabolite flux through the catabolic pathways is high in guard cells. In addition, other support is provided for the view that photoreduction of CO2 by these guard cells is absent.


2 Permanent address: Technische Universität München, Lehrstuhl für Botanik, Arcisstraße 21, D-8000 München 2, F. R. G.

1 Supported by a Department of Energy grant to W. H. O., Jr. and a travel grant from the Deutsche Forschungsgemeinschaft to R. H.




This article has been cited by other articles:


Home page
J Exp BotHome page
G. Tallman
Are diurnal patterns of stomatal movement the result of alternating metabolism of endogenous guard cell ABA and accumulation of ABA delivered to the apoplast around guard cells by transpiration?
J. Exp. Bot., September 1, 2004; 55(405): 1963 - 1976.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY THE PLANT CELL
Copyright © 1982 by the American Society of Plant Biologists