About the Lectin

A lectin isolated from the seed of the chick pea, Cicer arietinum, agglutinates papain treated human erythrocytes strongly. Untreated cells react weakly, and only in the presence of high concentrations of BSA. Several glycoproteins have been used as inhibitors; for example, human IgM and bovine fetuin will inhibit agglutination at less than 1µM. Ovalbumin was not inhibitory even at a concentration of 0.5mM. A number of mono- and disaccharides have been evaluated for their ability to inhibit agglutination. None were inhibitory even at concentrations as high as 150mM. In contrast to many other lectins, CPA is 3-4 times more active at 4°C than at room temperature. Pre-treatment with b-mercaptoethanol does not alter the electrophoretic pattern 1 . The lectin does not react with simple sugars and is therefore purified by ion-exhange chromatography according to procedures described by Kolberg, et al 1 . Partially purified CPA agglutinates leukocytes from various tyoes of leukaemia, but not peripheral blood cells from normal blood or from patients with non-leukaemic lymphoproliferative disorders 2 . The aglutination is inhibited by D-melibiose or D-raffinose. The FITC-conjugated lectin stained nuclei of immature, but not mature spermatocysts in rat testes 3 .

REFERENCES

  1. Kolberg, J., et al. (1983). Hoppe-Seyler’s Z. Physiol. Chem. 364: 655-664.
  2. Agarwal, S. and Agarwal, S. S. (1990) Ind. J. Med. Res. 92 : 38-42.
  3. Wine, R. N. and Chapin, R. E. (1997) J. Andrology 18 :71-79.

Product Characteristics

Buffer 0.01M Phosphate – 0.15M NaCl, pH 7.2-7.4.
Blood Group Nonspecific. Papain treated cells react more strongly.
Activity Poor reactivity with normal human erythrocytes, requiring 7.5% BSA. Less than 1 μg/ml will agglutinate papain treated cells.
Inhibitory Carbohydrate Not inhibited by simple sugars. Human IgM and bovine fetuin are potent inhibitors.
Molecular Weight 43,000 by gel filtration. A major band of MW = 26,000 appears on SDS-PAGE. Several minor low molecular weight bands may also appear.