Lectin from Bandeiraea simplicifolia (Griffonia simplicifolia) 

Agglutination activity is expressed in μg/mL and is determined from serial dilutions of a 1 mg/mL solution using phosphate buffered saline, pH 6.8, containing, for each lectin, calcium, magnesium, and manganese at different concentrations. This activity is the lowest concentration to agglutinate a 2% suspension of appropriate erythrocytes after 1 hr incubation at 25 °C.

BS-I has a major affinity for terminal α-D-galactosyl residues with a secondary affinity for terminal N-acetyl-α-D-galactosaminyl residues.¹

BS-I is a tetrameric lectin consisting of two types of subunits designated A and B. There are five BS-I isolectins with different subunit composition: BSI-B₄, BSI-AB₃, BSI-A₂B₂, BSI-A₃B and BSI-A₄. BSI-B₄ is blood group B specific and has an exclusive affinity for terminal α-D-galactosyl residues, whereas BSI-A₄ has blood group A specificity and has a major affinity for terminal N-acetyl-α-D-galactosaminyl residues.

Prepared from peroxidase type VI using a modification of the method of O'Sullivan, et al. Repurified by affinity chromatography after conjugation.

One unit will form 1 mg purpurogallin in 20 sec from pyrogallol at pH 6.0 at 20 °C.

Contains sodium citrate buffer salts and calcium chloride

lyophilized powder

<200 μg per mL agglutination activity (using human blood group B erythrocytes)

40-160 units/mg protein

Protein, ~95% modified Warburg-Christian

peroxidase conjugate

−20°C

1. Hayes, C. E., Goldstein, I. J. J. Biol. Chem. 249, 1904, (1974)

O'Sullivan, M. J., et al., A simple method for the preparation of enzyme-antibody conjugates. FEBS Lett. 95, 311-313, (1978) abstract

Murphy, L. A., Goldstein, I. J. J. Biol. Chem. 252, 4739, (1977)

Wood, C. Arch. Biochem. Biophys. 198, 1, (1979)

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