| Definition |
L-Asparaginases catalyse the hydrolysis of L-asparagine into L-aspartate and ammonia. The asparaginases isolated from Escherichia coli (EcA) and Erwinia chrysanthemi (EcA) are useful anti-leukaemic agents. Asparaginase treatment can be associated with severe side effects, which are believed to be associated with their glutaminase activity.(Asparaginase from Erwinia chrysanthemi; Erwinia L-asparaginase:),Erwinase is used in combination with other anti-neoplastic agents to treat acute lymphoblastic leukaemia. It may also be used in other neoplastic conditions where depletion of asparagine might be expected to have a useful effect. Patients receiving treatment with L-asparaginase from Escherichia coli, and who develop hypersensitivity to that enzyme may be able to continue treatment with Erwinase as the enzymes are immunologically distinct.Undesirable effects: Neurotoxicity, life-threatening sepsis and severe hypersensitivity have been described in patients treated with L-asparaginases. Other effects reported with both enzymes include fever; nausea; vomiting; CNS depression; hypersensitivity; acute pancreatitis and various plasma biochemical changes including increased BSP retention and elevation of bilirubin, SGOT, alkaline phosphatase and cholesterol levels; decreases in fibrinogen and some clotting factors. For these reasons, careful monitoring is therefore necessary and urine should be tested for glucose to exclude hyperglycaemia. Undesirable effects are generally reversible and are less common with Erwinia Lasparaginase than with E. coli asparaginase.
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