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 DDC exists 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
DOIs
StatePublished - Jan 1 1983

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ASJC Scopus subject areas

  • Biochemistry

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