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

doi:10.1016/0006-291X(74)90837-7

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 journal › Article › peer-review

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 language	English
Pages (from-to)	1301-1305
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	57
Issue number	4
DOIs	https://doi.org/10.1016/0006-291X(74)90837-7
Publication status	Published - 23 Apr 1974
Externally published	Yes

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AU - Udenfriend, Sidney

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AB - 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.

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

Abstract

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