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


     


Plant Physiology 94:960-969 (1990)
© 1990 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 Yang, Y.
Right arrow Articles by Steup, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Yang, Y.
Right arrow Articles by Steup, M.
Agricola
Right arrow Articles by Yang, Y.
Right arrow Articles by Steup, M.
Metabolism and Enzymology

Polysaccharide Fraction from Higher Plants which Strongly Interacts with the Cytosolic Phosphorylase Isozyme 1

I. Isolation and Characterization

Yi Yang and Martin Steup

Botanisches Institut der Westfälischen Wilhelms-Universität Münster, Schlossgarten 3, D-4400 Münster, Federal Republic of Germany

From leaves of Spinacia oleracea L. or from Pisum sativum L. and from cotyledons of germinating pea seeds a high molecular weight polysaccharide fraction was isolated. The apparent size of the fraction, as determined by gel filtration, was similar to that of dextran blue. Following acid hydrolysis the monomer content of the polysaccharide preparation was studied using high pressure liquid and thin layer chromatography. Glucose, galactose, arabinose, and ribose were the main monosaccharide compounds. The native polysaccharide preparation interacted strongly with the cytosolic isozyme of phosphorylase (EC 2.4.1.1). Interaction with the plastidic phosphorylase isozyme(s) was by far weaker. Interaction with the cytosolic isozyme was demonstrated by affinity electrophoresis, kinetic measurements, and by 14C-labeling experiments in which the glucosyl transfer from [14C]glucose 1-phosphate to the polysaccharide preparation was monitored.


1 Supported by grants from the Deutsche Forschungsgemeinschaft (Ste 217/7-1 and Ste 217/7-2) and from the Minister für Wissenschaft und Forschung des Landes Nordrhein-Westfalen.




This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
J. M. Steichen, R. V. Petty, and T. D. Sharkey
Domain Characterization of a 4-{alpha}-Glucanotransferase Essential for Maltose Metabolism in Photosynthetic Leaves
J. Biol. Chem., July 25, 2008; 283(30): 20797 - 20804.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
Y. Lu, J. M. Steichen, J. Yao, and T. D. Sharkey
The Role of Cytosolic {alpha}-Glucan Phosphorylase in Maltose Metabolism and the Comparison of Amylomaltase in Arabidopsis and Escherichia coli
Plant Physiology, November 1, 2006; 142(3): 878 - 889.
[Abstract] [Full Text] [PDF]


Home page
Plant Cell PhysiolHome page
J. Fettke, S. Poeste, N. Eckermann, A. Tiessen, M. Pauly, P. Geigenberger, and M. Steup
Analysis of Cytosolic Heteroglycans from Leaves of Transgenic Potato (Solanum tuberosum L.) Plants that Under- or Overexpress the Pho 2 Phosphorylase Isozyme
Plant Cell Physiol., December 1, 2005; 46(12): 1987 - 2004.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
S. E. Weise, K. S. Kim, R. P. Stewart, and T. D. Sharkey
{beta}-Maltose Is the Metabolically Active Anomer of Maltose during Transitory Starch Degradation
Plant Physiology, February 1, 2005; 137(2): 756 - 761.
[Abstract] [Full Text] [PDF]


Home page
Plant Cell PhysiolHome page
N. Schupp and P. Ziegler
The Relation of Starch Phosphorylases to Starch Metabolism in Wheat
Plant Cell Physiol., October 15, 2004; 45(10): 1471 - 1484.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
E. Baroja-Fernandez, F. J. Munoz, A. Zandueta-Criado, M. T. Moran-Zorzano, A. M. Viale, N. Alonso-Casajus, and J. Pozueta-Romero
Most of ADP{middle dot}glucose linked to starch biosynthesis occurs outside the chloroplast in source leaves
PNAS, August 31, 2004; 101(35): 13080 - 13085.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY THE PLANT CELL
Copyright © 1990 by the American Society of Plant Biologists