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


     


Plant Physiology 48:765-769 (1971)
© 1971 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 Ozbun, J. L.
Right arrow Articles by Preiss, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ozbun, J. L.
Right arrow Articles by Preiss, J.
Agricola
Right arrow Articles by Ozbun, J. L.
Right arrow Articles by Preiss, J.
Articles

Adenosine Diphosphoglucose-Starch Glucosyltransferases from Developing Kernels of Waxy Maize

J. L. Ozbun1, J. S. Hawker2 and Jack Preiss

a Department of Biochemistry and Biophysics, University of California, Davis, California 95616

Two adenosine diphosphoglucose: {alpha}-1,4-glucan {alpha}-4-glucosyl-transferases were extracted from kernels of waxy maize harvested 22 days after pollination and separated by gradient elution from a diethylaminoethyl-cellulose column. Both fractions could utilize amylopectin, amylose, glycogen, maltotriose and maltose as primers. The rate of glucose transfer from adenosine diphosphoglucose to rabbit liver glycogen of fraction II was 78% of the rate of glucose transfer to amylopectin, but with fraction I the rate of transfer of glucose to rabbit liver glycogen was 380% of that observed to amylopectin. Glucan synthesis in the absence of added primer was found in fraction I in the presence of 0.5 M sodium citrate and bovine serum albumin. The unprimed product was a methanol-precipitable glucan with principally {alpha}-1,4 linkages and some {alpha}-1,6 linkages, and its iodine spectrum was similar to that of amylopectin.


1 Present address: Vegetable Crops Department, Cornell University, Ithaca, N.Y. 14850.

2 Present address: Division of Horticultural Research, Common-wealth Scientific and Industrial Research Organization, Adelaide, Australia.




This article has been cited by other articles:


Home page
Plant Physiol.Home page
N. Fujita, M. Yoshida, N. Asakura, T. Ohdan, A. Miyao, H. Hirochika, and Y. Nakamura
Function and Characterization of Starch Synthase I Using Mutants in Rice
Plant Physiology, March 1, 2006; 140(3): 1070 - 1084.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY THE PLANT CELL
Copyright © 1971 by the American Society of Plant Biologists