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


     

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 (11)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Winefield, C. S.
Right arrow Articles by Farnden, KJF.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Winefield, C. S.
Right arrow Articles by Farnden, KJF.
Agricola
Right arrow Articles by Winefield, C. S.
Right arrow Articles by Farnden, KJF.

PLANT PHYSIOLOGY , Vol 104, Issue 2 417-423, Copyright © 1994 by American Society of Plant Biologists

MOLECULAR BIOLOGY AND GENE REGULATION

Cloning and Characterization of a cDNA Encoding Aspartate Aminotransferase-P1 from Lupinus angustifolius Root Tips

C. S. Winefield, B. D. Reddington, W. T. Jones, PHS. Reynolds and KJF. Farnden
Biochemistry Department, University of Otago, Dunedin, New Zealand (C.S.W., B.D.R., K.J.F.F.)

A root tip cDNA library, constructed in the [lambda] Zap II expression vector, was immunoscreened with a monoclonal antibody raised against aspartate aminotransferase-P1 from Lupinus angustifolius L. var Uniharvest. One 1452-base pair clone was isolated. The encoded protein sequence had high homology to both plant and animal aspartate aminotransferase sequences. The clone was converted to the phagemid form and expressed in Escherichia coli. The expressed protein was enzymically active and could be immuno-complexed with aspartate aminotransferase-P1-specific antibodies. The complete aspartate aminotransferase-P1 cDNA was cloned into the yeast expression vector pEMBL-yex4 and transformed into Saccharomyces cerevisiae strain BRSCS6, which possesses a mutated aspartate aminotransferase gene (the asp5 mutation). Complementation of the mutation was achieved using this construct.


This article has been cited by other articles:


Home page
 J Exp BotHome page
S. Silvente, A. Camas, and M. Lara
Molecular cloning of the cDNA encoding aspartate aminotransferase from bean root nodules and determination of its role in nodule nitrogen metabolism
J. Exp. Bot., June 1, 2003; 54(387): 1545 - 1551.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1994 by the American Society of Plant Biologists