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  • Title: Purification and partial characterization of a lectin from Euphorbia neriifolia latex.
    Author: Seshagirirao K, Prasad MN.
    Journal: Biochem Mol Biol Int; 1995 May; 35(6):1199-204. PubMed ID: 7492957.
    Abstract:
    A lectin was purified from Euphorbia neriifolia latex to homogeneity by affinity chromatography on Sepharose 4B. The protein appears to be a dimer with approximate M(r) of 60,000 on gel filtration and showing a single band at M(r) 32,000 in SDS-PAGE, and contains 12.3% carbohydrate. It agglutinated trypsinized human and rabbit erythrocytes, but not sheep erythrocytes. However, sialidase-treated sheep erythrocytes were agglutinated. The galactose and galactose containing sugars inhibited the heamagglutination with increased beta-anomeric specificity. The Euphorbia lectin possesses mitogenic activity with murine spleen lymphocytes but it does not inhibit protein synthesis in rabbit reticulocyte lysate.
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