The interaction of dopamine-β-hydroxylase with concanavalin a and its use in enzyme purification

Robert A. Rush, Paul E. Thomas, Shmuel H. Kindler, Sidney Udenfriend

Research output: Contribution to journalArticle

67 Citations (Scopus)

Abstract

Dopamine-β-hydroxylase forms a complex with concanavalin A and can be quantitatively dissociated from the complex with α-methyl-D mannoside. It can thus be separated from other chromaffin vesicle proteins that have no affinity for the lectin. Using this observation it was possible to purify the enzyme by a single passage through a column of concanavalin A-Sepharose. Analysis of the concentrated eluate by disc gel electrophoresis showed that the dopamine-β-hydroxy-last was 93% pure. The binding of this glycoprotein enzyme to concanavalin A indicates that the polysaccharide moiety is highly branched and contains α-D-mannopyranosyl and/or α-D-glucopyranosyl residues as the terminal sugars.

Original languageEnglish
Pages (from-to)1301-1305
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume57
Issue number4
DOIs
Publication statusPublished - 23 Apr 1974
Externally publishedYes

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