Science and Education Publishing Journal of Food and Nutrition Research 1 1 2013 09 24 Purification of an Antiproliferative Lectin from Erophaca Baetica (Leguminosae) Seeds 87 91 EN Cristina Megías Isabel Cortés-Giraldo Julio Girón-Calle Manuel Alaiz Javier Vioque Instituto de la Grasa (C.S.I.C.), Avda Padre García Tejero, Sevilla, SPAIN JFNR2013152 10.12691/jfnr-1-5-2 2013 09 10 2013 09 18 2013 09 24 A lectin has been purified from the seeds of Erophaca baetica, an endemic legume of the Mediterranean Region. The protein has been purified from an albumin extract by gel filtration chromatography, after realization that affinity chromatography using Sephadex G-50 did not retain any proteins. Characterization of this protein shows that it is a 60 kDa homodimeric glycoprotein with 235 mg sugars / g protein, and two 30 kDa subunits. Its amino acid composition is similar to those reported for the lectins of other related legumes such as Astragalus mongholicus. It agglutinates trypsinized erythrocytes, and inhibits proliferation of human leukemic THP-1 cells. Thus, this novel lectin may be of interest from a functional point of view due to its antiproliferative activity.