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Asparaginase from the testa of developing lupin and pea seeds.

Research output: Contribution to Journal/MagazineJournal article

<mark>Journal publication date</mark>08/1993
Issue number1
Number of pages6
Pages (from-to)51-56
Publication StatusPublished
<mark>Original language</mark>English


Potassium independent asparaginase has been purified from the testa of maturing seeds of Lupinus polyphyllus. The enzyme has a Mr of 71 × 103 and is composed of two subunits of Mr 35–36 × 103. Antisera raised against the purified asparaginase cross-reacted with a protein of similar characteristics isolated from the cotyledons and leaves of L. polyphyllus but no reaction was detected with extracts from the roots and nodules following Western blot analysis. Potassium dependent asparaginase was purified to a lesser extent from the testa of pea seeds and was shown to have a Mr of 61 × 103. The potassium independent and dependent enzymes appear to be distinct proteins with different immunological characteristics. The proportion of the two enzymes varies with plant species, organ and developmental age.