Purification of allantoinase from soybean seeds and production and characterization of anti-allantoinase antibodies.

Abstract:

: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.

journal_name

Plant Physiol

journal_title

Plant physiology

authors

Webb MA,Lindell JS

doi

10.1104/pp.103.4.1235

subject

Has Abstract

pub_date

1993-12-01 00:00:00

pages

1235-41

issue

4

eissn

0032-0889

issn

1532-2548

pii

103/4/1235

journal_volume

103

pub_type

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