Robinia pseudoacacia

About the Lectin

Seeds of black locust contains two lectins of similar reactivity, each of which is a homotetramer of 34 kDa or 29 kDa subunits that differ primarily in their number and occupancy of glycosylation sites 1 . Other workers have reported more complex subunit structures, possibly due to variation in the source and homogeniety of seeds 1-3 . The lectins bind to immobilized fetuin, but the carbohydrate specificity is complex since none of the simple mono- and disaccharides tested are inhibitors of agglutination 4 . Neuraminidase treated cells react more strongly than untreated human erythrocytes. Hemagglutination has been reported at concentrations of 10&#956g/ml, however the material supplied by EY Laboratories reacts with neuraminidase treated cells at a concentration of approximately 100&#956g/ml. A sialoglycoprotein found in the urine of pregnant women is a strong inhibitor of agglutination 5 . A glycopeptide is released after treatment with Pronase and trypsin, which is responsible for the agglutination activity of the lectin. A lectin has also been isolated from the bark of the black locust tree 6 . The seed and bark lectins are the products of two and three distinct genes, respectively 1 . RPA is a potent human T-cell activator 7 , and also selectively agglutinates Lancefield group C Streptococci 8 .

REFERENCES

  1. Van Damme, E.J.M., et al. (1995) Plant Mol. Biol. 29 : 1197-1210.
  2. Fleischmann, G. and Rudiger, H. (1986) Biol. Chem. Hoppe-Seyler 367 : 27-32.
  3. Wantyghem, J., et al. (1986) Biochem. J. 237 : 483-489.
  4. Bourrillon, R. and Font, J. (1968) Biochim. Biophys. Acta. 154: 28-39.
  5. Lemonnier, M., et al. (1972) Carbohydr. Res. 24: 323-331
  6. Broekaert, W. F., et al. (1984) Biochem. J. 221: 163-169.
  7. Sharif, A., et al. (1978) Immunology 35 : 643-649.
  8. Kellens, J.T. (1994) J. Med. Microbiol. 41 : 14-19.

Product Characteristics

Buffer 0.01M Phosphate – 0.15M NaCl, pH 7.2-7.4.
Blood Group Non-specific. Neuraminidase treated cells react more strongly than untreated cells.
Activity 100 μg/ml may be required to agglutinate neuraminidase treated red blood cells.
Inhibitory Carbohydrate Not inhibited by simple sugars
Molecular Weight Multiple bands between 25-50,000 Da by SDS‑PAGE.