Vicia palaestina Boiss. is an annual herb that grows in dry areas of eastern Mediterranean countries. It belongs to section Cracca subgenus Vicilla, which is characterized by having a high content in the non‐protein amino acid canavanine. The seeds from some of these vetches are also rich in lectins. The purification and characterization of a single‐chain lectin from the seeds of V. palaestina is described here. This lectin was the most abundant protein in albumin extracts. It has affinity for the glycoconjugate N‐acetylgalactosamine and inhibits proliferation of the cancerous Caco‐2 and THP‐1 cell lines. In addition to their high nutritional value, the seeds from V. palaestina represent a source of lectins with health promoting and pharmacological potential because of their antiproliferative activity.

Lectins are proteins or glycoproteins, which participate in various biological processes. The purpose of this study was to purify new lectin from Ruta montana roots. Lectin of Ruta montana has been purified from roots using ultrafiltration and precipitation with ammonium sulfate followed by gel filtration chromatography whereas protein estimation was done by Bradford’s method. Within sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS–PAGE) analysis, the extract exhibited three bands and one band after purification. The molecular weight of lectin was determined by SDS–PAGE and gel filtration chromatography, which was found to be a monomeric protein of approximately 28.8 kDa. The agglutination activity of Ruta montana lectins was stable within a temperature range from 4 to 50° C for 30 min and the pH range from 4.2 to 9. This study presents a natural source of lectins that can be used in several other studies due to its different biological activities.