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 Webb, M. A.
Right arrow Articles by Lindell, J. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Webb, M. A.
Right arrow Articles by Lindell, J. S.
Agricola
Right arrow Articles by Webb, M. A.
Right arrow Articles by Lindell, J. S.

PLANT PHYSIOLOGY , Vol 103, Issue 4 1235-1241, Copyright © 1993 by American Society of Plant Biologists

METABOLISM AND ENZYMOLOGY

Purification of Allantoinase from Soybean Seeds and Production and Characterization of Anti-Allantoinase Antibodies

M. A. Webb and J. S. Lindell
Department of Botany and Plant Pathology, Purdue University, West Lafayette, Indiana 47907-1155

Allantoinase catalyzes the hydrolysis of allantoin to allantoic acid, a reaction important in both biogenesis and degradation of ureides. Ureide production in cotyledons of germinating soybean (Glycine max L.) seeds has not been studied extensively but may be important in mobilizing nitrogen reserves. Allantoinase was purified approximately 2500-fold from a crude extract of soybean seeds by differential centrifugation, heat treatment, ammonium sulfate fractionation, ethanol fractionation, and fast protein liquid chromatography (Pharmacia) with Mono-Q and Superose columns. The purified enzyme had a subunit size of 30 kD. Polyclonal antibodies produced against the purified protein titrated allantoinase activity in a crude extract of seed proteins. Antibodies recognized the 30-kD band in western blot analysis of crude seed extracts, indicating that they were specific for allantoinase.


This article has been cited by other articles:


Home page
 J Exp BotHome page
C. D. Todd, P. A. Tipton, D. G. Blevins, P. Piedras, M. Pineda, and J. C. Polacco
Update on ureide degradation in legumes
J. Exp. Bot., January 1, 2006; 57(1): 5 - 12.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
S. B. Mulrooney and R. P. Hausinger
Metal Ion Dependence of Recombinant Escherichia coli Allantoinase
J. Bacteriol., January 1, 2003; 185(1): 126 - 134.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
A. Muñoz, P. Piedras, M. Aguilar, and M. Pineda
Urea Is a Product of Ureidoglycolate Degradation in Chickpea. Purification and Characterization of the Ureidoglycolate Urea-Lyase
Plant Physiology, February 1, 2001; 125(2): 828 - 834.
[Abstract] [Full Text]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1993 by the American Society of Plant Biologists