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PMID: 6405659 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Accurate assay of dopa decarboxylase by preventing nonenzymatic decarboxylation of dopa.

Analytical biochemistry ·Vol. 129 ·No. 2 ·1983-03-00 ·Pages 412-5

Okuno S, Fujisawa H

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.

MeSH Terms

Animals Aromatic-L-Amino-Acid Decarboxylases/analysis Decarboxylation Dihydroxyphenylalanine Dopa Decarboxylase/analysis Hydrogen-Ion Concentration Kidney Cortex/enzymology Swine

Chemicals

Dihydroxyphenylalanine Dopa Decarboxylase Aromatic-L-Amino-Acid Decarboxylases

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Okuno S

Fujisawa H

Article Info

Journal

Analytical biochemistry

Abbr.

Anal Biochem

ISSN

0003-2697

DOI

10.1016/0003-2697(83)90570-5

Published

1983-03-00

Pages

412-5

Language

English

Region

United States

NLM ID

0370535

Subset

External Links

PubMed source DOI: 10.1016/0003-2697(83)90570-5 View journal details

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Accurate assay of dopa decarboxylase by preventing nonenzymatic decarboxylation of dopa.

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