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Accurate assay of dopa decarboxylase by preventing nonenzymatic decarboxylation of dopa
Analytical Biochemistry
|March 1, 1983
Abstract:
The nonenzymatic decarboxylation of dopa was completely blocked by both 2-mercaptoethanol and EDTA together over the wide range of pH. This finding made it possible to measure the activity of dopa decarboxylase precisely even at an alkaline pH value. The pH optimum of dopa decarboxylase was found to be pH 7.0 and the Km value for dopa was determined to be 4 X 10(-5) M.