Abstract
1. 1. The biochemical properties of ornithine-δ-transaminase (OTA) from Schistosoma mansoni and Fasciola hepatica were compared. 2. 2. The OTA from both flukes could be solubilized to different degrees by various detergent mixtures. 3. 3. The pH optimum for the enzymatic activity was 8–8.5. 4. 4. The K m values of OTA from F. hepatica were 3.29 and 1.81 mM for ornithine and α-ketoglutarate, respectively, and of OTA from S. mansoni—1.53 and 2.07 mM. 5. 5. The enzyme showed the highest affinity for α-ketoglutarate from among seven keto acids evaluated. 6. 6. OTA was inhibited by known pyridoxal phosphate inhibitors as well as by several structural analogues of its two substrates.
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