Isolation of 3,4-dihydroxyphenylalanine-containing proteins using boronate affinity chromatography

Hawkins, Clifford J., Lavin, Martin F., Parry, David L. and Ross, Ian L. (1986) Isolation of 3,4-dihydroxyphenylalanine-containing proteins using boronate affinity chromatography. Analytical Biochemistry, 159 1: 187-190. doi:10.1016/0003-2697(86)90326-X


Author Hawkins, Clifford J.
Lavin, Martin F.
Parry, David L.
Ross, Ian L.
Title Isolation of 3,4-dihydroxyphenylalanine-containing proteins using boronate affinity chromatography
Journal name Analytical Biochemistry   Check publisher's open access policy
ISSN 0003-2697
Publication date 1986-11-15
Sub-type Article (original research)
DOI 10.1016/0003-2697(86)90326-X
Volume 159
Issue 1
Start page 187
End page 190
Total pages 4
Language eng
Subject 060199 Biochemistry and Cell Biology not elsewhere classified
Formatted abstract
A rapid procedure for the isolation of 3,4-dihydroxyphenylalanine-containing proteins has been developed in which the protein is selectively bound to a m-phenylboronate agarose column, and eluted with 1.0M ammonium acetate, pH 3.0. The method is based on the affinity of boronates for diols including catechol. The chromatography is carried out in the absence of oxygen to prevent oxidation of the catechol. Other proteins are eluted beforehand with 0.25M ammonium acetate, pH 8.5, or for glycoproteins with a Tris buffer containing 0.2M sorbitol, pH 8.5.
Keyword protein purification
structural proteins
DOPA-proteins
iron-binding proteins
ascidians
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Institute for Molecular Bioscience - Publications
 
Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 25 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 27 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Fri, 19 Feb 2010, 19:48:12 EST by Ms Laura Mctaggart on behalf of Institute for Molecular Bioscience