Modification of the Biological Properties of Plant Lectins by Chemical Crosslinking

  • Reuben Lotan
  • Nathan Sharon
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 86A)


Soybean agglutinin, a glycoprotein lectin (m.w. 120,000, two N-acetyl-D-galactosamine binding sites/mole) was crosslinked with glutaraldehyde. Polymers (m.w. ⩾240,000). thus obtained were separated from uncrosslinked molecules by gel filtration and found to be polyvalent with respect to sugar binding (⩾4 binding sites/mole). Soybean agglutinin polymers exhibited high agglutinating activity toward erythrocytes and lymphocytes and triggered mitogenic stimulation of the latter cells, while the uncrosslinked divalent soybean agglutinin was a weaker agglutinin and failed to stimulate lymphocytes. Similar activities were found with aggregates of soybean agglutinin which formed upon lyophilization and storage of the lectin.

The effect of crosslinking of soybean agglutinin on its activities is assumed to be the result of increase in valency of the divalent molecule by conversion into multivalent polymers. Polyvalent soybean agglutinin is more efficient in forming multiple crossbridges between adjacent cells which lead to cell agglutination. Stimulation of lymphocytes may require crosslinkage and/or topographic redistribution of cell surface receptors; this requirement is satisfied by the poly- but not by the divalent lectin. The effect of crosslinking of other lectins, such as concanavalin A, phytohemagglutinin and the pokeweek mitogens, on their biological properties is discussed.


Lima Bean Hemagglutinating Activity Lymphocyte Stimulation Sephadex Column Agglutinate Activity 
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Copyright information

© Plenum Press, New York 1977

Authors and Affiliations

  • Reuben Lotan
    • 1
  • Nathan Sharon
    • 1
  1. 1.Department of BiophysicsThe Weizmann Institute of ScienceRehovotIsrael

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