Purification, Characterization, and Antiproliferative Activity of a Single-Chain Lectin from Vicia palaestina
Youssef Elamine1, Verenice Torres-Salas2, Alima Messai1
1Food Phytochemistry Department, Instituto de la Grasa (C.S.I.C.), Campus Universidad Pablo de Olavide, Carretera de Utrera Km 1, 41089, Sevilla, Spain.
Abstract:
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.
