Stabilization of immobilized lectin columns by crosslinking with glutaraldehyde

Analytical Biochemistry
M G ScherR J Bloch

Abstract

Procedures to purify membrane proteins usually require the use of detergents and often include affinity chromatography on lectin columns. Some detergents, especially denaturing detergents such as sodium dodecyl sulfate (SDS), can interfere with affinity chromatography by inactivating the bound lectin or by eluting it from the column together with the material of interest. We have developed a procedure that stabilizes lectin-column matrices by crosslinking with glutaraldehyde. This procedure does not impair the binding capacity of the immobilized lectin. It permits subsequent elution by SDS of bound glycoproteins without coelution of lectin subunits.

Citations

Mar 6, 2008·The Journal of Histochemistry and Cytochemistry : Official Journal of the Histochemistry Society·Luz Marina AcevedoMoise Bendayan
Sep 1, 1994·Asia-Oceania Journal of Obstetrics and Gynaecology·E HorimotoR Kudo
Aug 31, 2019·BioMed Research International·Rafael de Oliveira ResendeErnesto Akio Taketomi
Nov 18, 2020·The Journal of Infectious Diseases·Relber Aguiar GonçalesFernando Rodrigues
Aug 1, 1991·Protein Expression and Purification·C A Doige, F J Sharom

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