Abstract
A method is presented for the isolation of a lectin from a Japanese cultivar of Phaseolus vulgaris seed by an affinity chromatography on the heat-denaturated porcine thyroglobulin Sepharose. The lectin is a glycoprotein whose molecular weight is 120,000; it consists of four apparently identical subunits, held together by non-covalent forces. The isoelectric point is 5.5 and the sedimentation constant is 6.66 S at pH 5.3. The lectin is nonspecific in agglutination for any types of human erythrocytes. The lectin induces mitosis in human lymphocytes at concentration between 10 and 100 µg per 3×108 lymphocytes. The hemagglutinating and mitogenic activities are inhibited by N-acetyl-d-galactosamine and some simple sugars.
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