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5-Aminolevulinate dehydratase (ALAD) from spinach (Spinatia oleracea) was isolated by affinity purification on an immunoabsorbens with a yield of 70 to 80% of the activity in the crude enzyme preparation. The enzyme eluted from the immunoabsorbens was pure as judged by poly­ acrylamide gel electrophoresis and is a hexamer with a subunit molecular weight of about 50000. Enzyme bound to the immunoabsorbens was able to synthesize porphobilinogen in a continuous manner. Owing to the lability of the enzyme and its low abundance in plant tissue, we have been unable to obtain similar yields of purified enzyme using classical purification procedures.

Highly Efficient Purification of the Labile Plant Enzyme 5-Aminolevulinate Dehydratase (EC 4.2.1.24) by Means of Monoclonal Antibodies