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Purification, Characterization, and Antiproliferative Activity of a Single‐Chain Lectin from Vicia palaestina (Fabaceae) Seeds
Author(s) -
Elamine Youssef,
TorresSalas Verenice,
Messai Alima,
GirónCalle Julio,
Alaiz Manuel,
Vioque Javier
Publication year - 2021
Publication title -
chemistry and biodiversity
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.427
H-Index - 70
eISSN - 1612-1880
pISSN - 1612-1872
DOI - 10.1002/cbdv.202000827
Subject(s) - lectin , chemistry , fabaceae , glycoconjugate , biochemistry , subgenus , vicia faba , canavanine , protein subunit , amino acid , botany , biology , arginine , gene , genus
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.