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


     


This Article
Right arrow Full Text
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 (25)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Wischmann, B.
Right arrow Articles by Lindberg Møller, B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Wischmann, B.
Right arrow Articles by Lindberg Møller, B.
Agricola
Right arrow Articles by Wischmann, B.
Right arrow Articles by Lindberg Møller, B.

In Vitro Biosynthesis of Phosphorylated Starch in Intact Potato Amyloplasts1

Bente Wischmann*, Tom Hamborg Nielsen, and Birger Lindberg Møller

Plant Biochemistry Laboratory, Department of Plant Biology, The Royal Veterinary and Agricultural University, 40 Thorvaldsensvej, DK-1871 Frederiksberg C, Copenhagen, Denmark

Intact amyloplasts from potato (Solanum tuberosum L.) were used to study starch biosynthesis and phosphorylation. Assessed by the degree of intactness and by the level of cytosolic and vacuolar contamination, the best preparations were selected by searching for amyloplasts containing small starch grains. The isolated, small amyloplasts were 80% intact and were free from cytosolic and vacuolar contamination. Biosynthetic studies of the amyloplasts showed that [1-14C]glucose-6-phosphate (Glc-6-P) was an efficient precursor for starch synthesis in a manner highly dependent on amyloplast integrity. Starch biosynthesis from [1-14C]Glc-1-P in small, intact amyloplasts was 5-fold lower and largely independent of amyloplast intactness. When [33P]Glc-6-P was administered to the amyloplasts, radiophosphorylated starch was produced. Isoamylase treatment of the starch followed by high-performance anion-exchange chromatography with pulsed amperometric detection revealed the separated phosphorylated alpha -glucans. Acid hydrolysis of the phosphorylated alpha -glucans and high-performance anion-exchange chromatography analyses showed that the incorporated phosphate was preferentially positioned at C-6 of the Glc moiety. The incorporation of radiolabel from Glc-1-P into starch in preparations of amyloplasts containing large grains was independent of intactness and most likely catalyzed by starch phosphorylase bound to naked starch grains.


1   This study was supported by The Danish Center for Plant Biotechnology, by the FØTEK Program, and by The Nordic Fund for Technology and Industrial Development.
*   Corresponding author; e-mail bw{at}kvl.dk; fax 45-3528-3333.

Plant Physiol. (1999) 119: 455-462
Copyright Clearance Center:   0032-0889/99/119//08
© 1999 American Society of Plant Physiologists




This article has been cited by other articles:


Home page
Plant Physiol.Home page
V. T. Valkov, N. Scotti, S. Kahlau, D. MacLean, S. Grillo, J. C. Gray, R. Bock, and T. Cardi
Genome-Wide Analysis of Plastid Gene Expression in Potato Leaf Chloroplasts and Tuber Amyloplasts: Transcriptional and Posttranscriptional Control
Plant Physiology, August 1, 2009; 150(4): 2030 - 2044.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
R. Mikkelsen, K. E. Mutenda, A. Mant, P. Schurmann, and A. Blennow
{alpha}-Glucan, water dikinase (GWD): A plastidic enzyme with redox-regulated and coordinated catalytic activity and binding affinity
PNAS, February 1, 2005; 102(5): 1785 - 1790.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
O. Kotting, K. Pusch, A. Tiessen, P. Geigenberger, M. Steup, and G. Ritte
Identification of a Novel Enzyme Required for Starch Metabolism in Arabidopsis Leaves. The Phosphoglucan, Water Dikinase
Plant Physiology, January 1, 2005; 137(1): 242 - 252.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
G. Ritte, A. Scharf, N. Eckermann, S. Haebel, and M. Steup
Phosphorylation of Transitory Starch Is Increased during Degradation
Plant Physiology, August 1, 2004; 135(4): 2068 - 2077.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
E. M. Farre, A. Tiessen, U. Roessner, P. Geigenberger, R. N. Trethewey, and L. Willmitzer
Analysis of the Compartmentation of Glycolytic Intermediates, Nucleotides, Sugars, Organic Acids, Amino Acids, and Sugar Alcohols in Potato Tubers Using a Nonaqueous Fractionation Method
Plant Physiology, October 1, 2001; 127(2): 685 - 700.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
N. Gerrits, S. C.H.J. Turk, K. P.M. van Dun, S. H.D. Hulleman, R. G.F. Visser, P. J. Weisbeek, and S. C.M. Smeekens
Sucrose Metabolism in Plastids
Plant Physiology, February 1, 2001; 125(2): 926 - 934.
[Abstract] [Full Text]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1999 by the American Society of Plant Biologists