PMID: 6405659Mar 1, 1983Paper

Accurate assay of dopa decarboxylase by preventing nonenzymatic decarboxylation of dopa

Analytical Biochemistry
S Okuno, H Fujisawa

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.

References

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Citations

Jun 15, 1990·Biochemical Pharmacology·W P MelegaJ R Barrio
Sep 15, 1986·Clinica Chimica Acta; International Journal of Clinical Chemistry·F BoomsmaM A Schalekamp
Jan 1, 1988·The International Journal of Biochemistry·R I BrinkworthP R Andrews
Oct 1, 1991·International Journal for Parasitology·J Walker, J Barrett
Sep 1, 1992·Neurochemistry International·K P GudehithluM Hadjiconstantinou
Mar 1, 1990·Journal of Neurochemistry·Z L RossettiM Hadjiconstantinou
Jan 1, 1990·European Journal of Cancer : Official Journal for European Organization for Research and Treatment of Cancer (EORTC) [and] European Association for Cancer Research (EACR)·M J EverardI E Smith
Feb 1, 1989·Journal of Neurochemistry·Z RossettiM Hadjiconstantinou
Sep 1, 1990·Journal of Cerebral Blood Flow and Metabolism : Official Journal of the International Society of Cerebral Blood Flow and Metabolism·J ReithA Gjedde

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