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Asian Journal of Biochemistry
  Year: 2010 | Volume: 5 | Issue: 3 | Page No.: 145-153
DOI: 10.3923/ajb.2010.145.153
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Isolation, Purification and Characterization of a Lectin from a Local Kashmiri Variety of Soybean (Glycine max)

H. Bashir, T. Khan, A. Masood and R. Hamid

A purification scheme was developed to purify a lectin from the seeds of a local Kashmiri variety of 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 Lowry’s 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.
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How to cite this article:

H. Bashir, T. Khan, A. Masood and R. Hamid, 2010. Isolation, Purification and Characterization of a Lectin from a Local Kashmiri Variety of Soybean (Glycine max). Asian Journal of Biochemistry, 5: 145-153.

DOI: 10.3923/ajb.2010.145.153






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