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A Fluorometric Assay for l-Asparaginase Activity and Monitoring of l-Asparaginase Therapy

✍ Scribed by Päivi Ylikangas; Ilkka Mononen

Publisher
Elsevier Science
Year
2000
Tongue
English
Weight
66 KB
Volume
280
Category
Article
ISSN
0003-2697

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✦ Synopsis

The antineoplastic enzyme L-asparaginase is commonly used for the induction of remission in acute lymphoblastic leukemia (ALL). There is no simple method available for measuring the activity of this highly toxic drug. We incubated L-asparaginase from Erwinia chrysanthemi with L-aspartic acid ␤-(7-amido-4-methylcoumarin) and measured the release of 7amino-4-methylcoumarin fluorometrically for 30 -300 min. The rate of the hydrolysis of the substrate was linear over a 50-fold range of the concentration of the enzyme. With increasing substrate concentration, the enzyme showed a saturable kinetic pattern with V max of 0.547 (SD 0.059) M/min/mg of enzyme (n ‫؍‬ 3) and K m of 0.302 (SD 0.095) mM (n ‫؍‬ 3). This assay enables rapid analysis of L-asparaginase activity in biological samples and it can be used, for example, for monitoring of L-asparaginase activity in serum of ALL patients during their L-asparaginase therapy.

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