@article{jfnr2013152,
author={{Meg¨ªas, Cristina and Cort¨¦s-Giraldo, Isabel and Gir¨®n-Calle, Julio and Alaiz, Manuel and Vioque, Javier},
title={Purification of an Antiproliferative Lectin from <i>Erophaca </i><i>B</i><i>aetica</i> (Leguminosae) Seeds},
journal={Journal of Food and Nutrition Research},
volume={1},
number={5},
pages={87--91},
year={2013},
url={http://pubs.sciepub.com/jfnr/1/5/2},
abstract={A lectin has been purified from the seeds of <i>Erophaca baetica</i>, 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 <i>Astragalus mongholicus</i>. 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.},
doi={10.12691/jfnr-1-5-2}
publisher={Science and Education Publishing}
}