Use of radiolabeled monofluoromethyl-dopa to define the subunit structure of human L-dopa decarboxylase

Rhoda Maneckjee, Stephen B Baylin

Research output: Contribution to journalArticle

Abstract

Human L-Dopa decarboxylase (L-aromatic amino acid decarboxylase, DDC) has been purified from pheochromocytoma tissue, a benign tumor of the catecholamine-synthesizing cells of the adrenal medulla. The binding characteristics of a new radiolabeled enzyme-activated suicide inhibitor of DDC ([3H]monofluoromethyl-Dopa, [3H]MFMD) have been established, and the covalent linkage of the inhibitor to the enzyme has been used to identify that human DDCexists as a dimer of a 50-kDa subunit. An antibody to human DDC identically precipitates the enzyme activity from different human, rat, and mouse tissues. Our data demonstrate the value of [3H]MFMD for probing the structure of DDC and facilitating the purification of this enzyme, and further emphasize the high degree of conservation of the DDC molecule over a wide variety of species.

Original languageEnglish (US)
Pages (from-to)6058-6063
Number of pages6
JournalBiochemistry®
Volume22
Issue number26
StatePublished - 1983

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Dopa Decarboxylase
Levodopa
Enzymes
Aromatic-L-Amino-Acid Decarboxylases
Tissue
Adrenal Medulla
Enzyme activity
Pheochromocytoma
Enzyme Inhibitors
Human Activities
Dimers
Suicide
Catecholamines
Purification
Rats
Tumors
Precipitates
Conservation
Molecules
Antibodies

ASJC Scopus subject areas

  • Biochemistry

Cite this

Use of radiolabeled monofluoromethyl-dopa to define the subunit structure of human L-dopa decarboxylase. / Maneckjee, Rhoda; Baylin, Stephen B.

In: Biochemistry®, Vol. 22, No. 26, 1983, p. 6058-6063.

Research output: Contribution to journalArticle

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