Abstract
Two hemagglutinating components purified from the lima bean and composed of identical 62,000-molecular-weight subunits have mitogenic activity in normal and leukemic human lymphocyte cultures. Component II (247,000 molecular weight), a tetramer with four saccharide binding sites, is severalfold more active than component III (124,000 molecular weight), a dimer with two binding sites per molecule, as a mitogen for normal lymphocytes. Component II also stimulates mitogenesis in populations of cultured leukemic lymphocytes and appears to have greater activity than phytohemagglutinin-P in leukemic lymphocyte cultures obtained from some patients. Lima bean component III has minimal mitogenic activity toward leukemic lymphocytes. Components II and III appear to compete for the same cell-surface binding sites, but component II has a much greater capacity than component III to trigger DNA synthesis at low concentrations (2.5-25 μg/ml) in normal lymphocyte cultures. These results suggest that the mitogenic activity of lima bean lectin components is directly related to their valence.
Keywords: phytohemagglutinin-P, cell surface receptors, valency
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