Academic Journals Database
Disseminating quality controlled scientific knowledge

Isolation, Purification and Characterization of a Lectin from a Local Kashmiri Variety of Soybean (Glycine max)

Author(s): H. Bashir | T. Khan | A. Masood | R. Hamid

Journal: Asian Journal of Biochemistry
ISSN 1815-9923

Volume: 5;
Issue: 3;
Start page: 145;
Date: 2010;
VIEW PDF   PDF DOWNLOAD PDF   Download PDF Original page

Keywords: N-Acetyl-galactosamine | ligand | Affinity chromatography | Soybean lectin

Glycine max (soybean). The lectin that specifically binds to N- acetyl galactosamine was purified to electrophoretic homogeneity by affinity chromatography on CNBr activated Sepharose 6B column. Human blood group A, B, O and AB erythrocytes were used for agglutination assay and the sugar specificity was determined by hemagglutination inhibition assay. Protein estimation was done by Lowrys method and analysis was done by PAGE both under native conditions and in presence of SDS. The purified soybean lectin (SBL) showed equal agglutination with all four types of blood groups i.e., A, B, O and AB. Hemagglutinating activity of the lectin is inhibited by N- acetyl galactosamine and galactose and other carbohydrates containing the galactopyranosyl residue. The purified lectin gave a single symmetric protein peak on gel filtration chromatography showing a molecular weight of 110 kDa and when subjected to native PAGE, showed a single protein band. A single band of 30 kDa was obtained upon SDS-PAGE, establishing that the lectin is composed of similar subunits i.e., it is a homotetramer.A tetrameric galactose specific lectin that shows equal activity with all blood type human erythrocytes was purified and characterized from a Kashmiri variety of soybean.]]>
RPA Switzerland

Robotic Process Automation Switzerland


Tango Jona
Tangokurs Rapperswil-Jona