Purification and partial characterization of a mitogenic lectin from the latex of Euphorbia marginata
1993
Stirpe, F. | Licastro, F. | Morini, M.C. | Parente, A. | Savino, G. | Abbondanza, A. | Bolognesi, A. | Falasca, A.I. | Rossi, C.A.
A lectin was purified from the latex of Euphorbia marginata by affinity chromatography on acid-treated Sepharose 6B and elution with lactose. The lectin is a glycoprotein composed of two identical subunits with Mr 30000, 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 strongly mitogenic for human T-lymphocytes and induces the release of interleukin-1beta and tumor necrosis factor-alpha from cultured mononuclear cells.
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