Lectin-Associated Proteins from the Seeds ofLeguminosae

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Abstract
The seeds of Pisum sativum (pea), Canavalia ensiformis, Vicia faba, V. sativa and Ricinus communis contain proteins which are associated to the respective lectins (lectin binders). The lectin binders from P. sativum and C. ensiformis were studied more closely. Both are single proteins not resembling the variety of membrane glycoproteins found in animals and plants which bind to lectins. The pea lectin binder is a tetrameric glycoprotein composed of identical subunits of the MW 51,000. Its interaction with the lectin is abolished by acidic buffers or by glucose. The concanavalin A binder, which does not contain sugar, is composed on 1 kind of subunit, MW of 35,000. As in the case of the pea lectin binder, glucose and acid dissociate the lectin-lectin binder complex, but in contrast to the pea lectin binder low NaCl concentrations also cause this effect. During germination and growth, the concanavalin A binder appears in the roots.