F. Stirpe et al., PURIFICATION AND PARTIAL CHARACTERIZATION OF A MITOGENIC LECTIN FROM THE LATEX OF EUPHORBIA-MARGINATA, Biochimica et biophysica acta, 1158(1), 1993, pp. 33-39
A lectin was purified from the latex of Euphorbia marginata by affinit
y chromatography on acid-treated Sepharose 6B and elution with lactose
. The lectin is a glycoprotein composed of two identical subunits with
M(r) 30 000, approx. The haemagglutinating activity of the lectin is
not specific for any human blood group, and is inhibited by galactose
and galactose-containing sugars and by gentiobiose. The lectin is stro
ngly mitogenic for human T-lymphocytes and induces the release of inte
rleukin-1beta and tumor necrosis factor-alpha from cultured mononuclea
r cells.