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


     


Plant Physiology 57:63-68 (1976)
© 1976 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 Sowokinos, J. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sowokinos, J. R.
Agricola
Right arrow Articles by Sowokinos, J. R.
Articles

Pyrophosphorylases in Solanum tuberosum

I. Changes in ADP-Glucose and UDP-Glucose Pyrophosphorylase Activities Associated with Starch Biosynthesis during Tuberization, Maturation, and Storage of Potatoes 1

Joseph R. Sowokinos2

a Department of Horticultural Sciences and Plant Physiology, University of Minnesota, St. Paul, Minnesota 55101

Changes in ADP-glucose and UDP-glucose pyrophosphorylase activities were followed during tuber development of Solanum tuberosum and prolonged storage at 4 and 11 C. Potato tuberization was accompanied by a sharp increase in starch synthesis simultaneous with a marked rise in ADP-glucose pyrophosphorylase activity. When tubers reached an average diameter of 1 centimeter (0.5 gram average tuber weight) and had already established 58% starch on a dry weight basis, ADP-glucose pyrophosphorylase increased 16- to 24-fold over its activity seen in low starch containing stolon tissue. During this same period UDP-glucose pyrophosphorylase increased approximately 2- to 3-fold. Although participation of UDP-glucose in starch formation can not be neglected, it is suggested that the onset of rapid non-photosynthetic potato tuber starch biosynthesis may be closely related to the simultaneous increase in ADP-glucose pyrophosphorylase activity.

Evidence that UDP-glucose and ADP-glucose pyrophosphorylases are separate protein entities was indicated by their (a) activity ratio variations during tuber development and storage, (b) extraction stabilities, (c) morphological localization, (d) separation with ammonium sulfate, (e) pH optima, and (f) differential activation with 3-P-glycerate.


2 Present address: Red River Valley Potato Research Laboratory, Box 113, East Grand Forks, Minnesota 56721, a laboratory cooperatively operated by the North Central Region Agricultural Research Service, USDA; Minnesota Agricultural Experiment Station; North Dakota Agricultural Experiment Station; and the Red River Valley Potato Growers' Association.

1 Agricultural Experiment Station. University of Minnesota Scientific Journal Series No. 9081.




This article has been cited by other articles:


Home page
Plant Physiol.Home page
S. K. Boehlein, A. K. Sewell, J. Cross, J. D. Stewart, and L. C. Hannah
Purification and Characterization of Adenosine Diphosphate Glucose Pyrophosphorylase from Maize/Potato Mosaics
Plant Physiology, July 1, 2005; 138(3): 1552 - 1562.
[Abstract] [Full Text] [PDF]


Home page
Plant Cell PhysiolHome page
E. Baroja-Fernandez, F. J. Munoz, T. Saikusa, M. Rodriguez-Lopez, T. Akazawa, and J. Pozueta-Romero
Sucrose Synthase Catalyzes the de novo Production of ADPglucose Linked to Starch Biosynthesis in Heterotrophic Tissues of Plants
Plant Cell Physiol., May 15, 2003; 44(5): 500 - 509.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
D. C. Fulton, A. Edwards, E. Pilling, H. L. Robinson, B. Fahy, R. Seale, L. Kato, A. M. Donald, P. Geigenberger, C. Martin, et al.
Role of Granule-bound Starch Synthase in Determination of Amylopectin Structure and Starch Granule Morphology in Potato
J. Biol. Chem., March 22, 2002; 277(13): 10834 - 10841.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
T. Fritzius, R. Aeschbacher, A. Wiemken, and A. Wingler
Induction of ApL3 Expression by Trehalose Complements the Starch-Deficient Arabidopsis Mutant adg2-1 Lacking ApL1, the Large Subunit of ADP-Glucose Pyrophosphorylase
Plant Physiology, June 1, 2001; 126(2): 883 - 889.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
A. Wingler, T. Fritzius, A. Wiemken, T. Boller, and R. A. Aeschbacher
Trehalose Induces the ADP-Glucose Pyrophosphorylase Gene, ApL3, and Starch Synthesis in Arabidopsis
Plant Physiology, September 1, 2000; 124(1): 105 - 114.
[Abstract] [Full Text]


Home page
Plant Physiol.Home page
B. Wischmann, T. Hamborg Nielsen, and B. Lindberg Møller
In Vitro Biosynthesis of Phosphorylated Starch in Intact Potato Amyloplasts
Plant Physiology, February 1, 1999; 119(2): 455 - 462.
[Abstract] [Full Text]


Home page
Plant Physiol.Home page
J. Sun, T. W. Okita, and G. E. Edwards
Modification of Carbon Partitioning, Photosynthetic Capacity, and O2 Sensitivity in Arabidopsis Plants with Low ADP-Glucose Pyrophosphorylase Activity
Plant Physiology, January 1, 1999; 119(1): 267 - 276.
[Abstract] [Full Text]


Home page
Proc. Natl. Acad. Sci. USAHome page
M. Rodriguez-Lopez, E. Baroja-Fernandez, A. Zandueta-Criado, and J. Pozueta-Romero
Adenosine diphosphate glucose pyrophosphatase: A plastidial phosphodiesterase that prevents starch biosynthesis
PNAS, July 18, 2000; 97(15): 8705 - 8710.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1976 by the American Society of Plant Biologists