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

Plant Physiol. 1993 December; 103(4): 1235–1241.

PMCID: PMC159111

M A Webb and J S Lindell

Department of Botany and Plant Pathology, Purdue University, West Lafayette, Indiana 47907-1155.

This article has been cited by other articles in PMC.

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.

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