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 Physioljournal_title
Plant physiologyauthors
Webb MA,Lindell JSdoi
10.1104/pp.103.4.1235subject
Has Abstractpub_date
1993-12-01 00:00:00pages
1235-41issue
4eissn
0032-0889issn
1532-2548pii
103/4/1235journal_volume
103pub_type
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