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The TMP kinase activity was measured spectrophotometrically using an enzyme-coupling assay. The assay is based on the decrease in absorbance at 335 nm due to conversion of NADH to NAD. The activity solution contained essential activity elements as KCL, MgCl2 as well as coupling enzymes 2U pyruvate kinase, 2U lactate dehydrogenase and their forerunner phosphoenolpyruvate [1, 2]. For assessment of inhibitors, the initial reaction rates were measured in the presence and absence of inhibitors as previously described [2, 6, 7].
Copyright and License information: ©2019 Kandeel et al
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