Properties of a Lectin Purified from the Seeds ofCicer arietinum

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Abstract
A lectin was isolated from seed extracts of C. arietinum by (NH4)2SO4 precipitation and subsequent ion exchange chromatography gel filtration. Affinity chromatography on desialated human IgM coupled to AH-Sepharose was also performed, but the amount bound was very low. The lectin has a MW of .apprx. 44,000 Da [daltons], as determined by ultracentrifugation and gel filtration. Dodecyl sulfate polyacrylamide-gel electrophoresis showed 1 band corresponding to a MW of 26,000 Da. N-Terminal amino acid sequence analyses indicate only 1 type of chain, suggesting that the lectin is probably dimeric. The amino acid composition is given. Propainized human erythrocytes of the different ABO groups were agglutinated equally well by the Cicer lectin; untreated cells reacted weakly and only in the presence of bovine serum albumin. Simple sugars did not inhibit the agglutination, but some glycoproteins did inhibit. The lectin is probably nonmitogenic against human lymphocytes. Antigen analyses in an enzyme-linked immunosorbent assay (ELISA) showed a weak cross-reaction between Cicer and the lectins in the Vicieae tribe. These physiochemical and antigenic studies of the Cicer lectin support the botanical reasons recently given for removing the genus Cicer from the Vicieae tribe.

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