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


     


Plant Physiology 69:117-121 (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 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 (48)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Gross, K. C.
Right arrow Articles by Pharr, D. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Gross, K. C.
Right arrow Articles by Pharr, D. M.
Agricola
Right arrow Articles by Gross, K. C.
Right arrow Articles by Pharr, D. M.
Articles

A Potential Pathway for Galactose Metabolism in Cucumis sativus L., A Stachyose Transporting Species 1

Kenneth C. Gross2 and David M. Pharr

Department of Horticultural Science, North Carolina State University, Raleigh, North Carolina 27650

Conversion of [14C]galactose (Gal) 1-P, UDP-[14C]Gal, or UDP-[14C]glucose to [14C]sucrose was observed when cell-free homogenates of cucumber (Cucumis sativus L.) fruit peduncles were incubated with individual 14C-labeled substrates, appropriate cofactors, and fructose. The sucrose product was labeled only in the glucose moiety. Conversion of [14C]Gal-1-P to [14C]sucrose was catalyzed by extracts of peduncles from all other stachyose transporting species tested, as well as green bean (a sucrose transporter) but was not catalyzed by peduncle extracts from three other sucrose transporting species. In cucumber, the ability of extracts to form [14C]sucrose from [14C]Gal-1-P was greater when peduncles were harvested from growing fruit than from unpollinated ovaries. [14C]Sucrose formation from [14C]Gal-1-P was inhibited by Mg · PPi, Mg · UDP, UMP, and sucrose. {alpha}-Galactosidase, galactokinase, UDP-gal pyrophosphorylase, UDP-Gal-4'-epimerase, UDP-glucose pyrophosphorylase, and sucrose synthase activities were detected in peduncle extracts. Neither sucrose phosphate synthetase nor hexose-1-P uridyltransferase were detected. Peduncle tissue contained a small pool of free galactose. These results suggest a potential pathway for the metabolism of galactose moieties hydrolyzed from stachyose, the major sugar transported by cucumber plants.


2 This work is a portion of a thesis submitted by the first author in partial fulfillment for the PhD degree.

1 Supported in part by funds from United States Department of Agriculture, Science and Education Administration cooperative agreement No. 58-7B30-9-140. Paper 6885 of the Journal Series of the North Carolina Agricultural Research Service, Raleigh, NC. The use of trade names in this publication does not imply endorsement by the North Carolina Agricultural Research Service of products named, nor criticism of similar ones not mentioned.




This article has been cited by other articles:


Home page
Plant Physiol.Home page
N. Dai, M. Petreikov, V. Portnoy, N. Katzir, D. M. Pharr, and A. A. Schaffer
Cloning and Expression Analysis of a UDP-Galactose/Glucose Pyrophosphorylase from Melon Fruit Provides Evidence for the Major Metabolic Pathway of Galactose Metabolism in Raffinose Oligosaccharide Metabolizing Plants
Plant Physiology, September 1, 2006; 142(1): 294 - 304.
[Abstract] [Full Text] [PDF]


Home page
J. Gen. Virol.Home page
I. M. Moreno, J. R. Thompson, and F. Garcia-Arenal
Analysis of the systemic colonization of cucumber plants by Cucumber green mottle mosaic virus
J. Gen. Virol., March 1, 2004; 85(3): 749 - 759.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
Z. Gao and A. A. Schaffer
A Novel Alkaline alpha -Galactosidase from Melon Fruit with a Substrate Preference for Raffinose
Plant Physiology, March 1, 1999; 119(3): 979 - 988.
[Abstract] [Full Text]




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