Purification and Characterization of a Mitogenic Lectin and a Lectin-Binding Protein fromVicia sativa

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Abstract
From the seeds of V. sativa, a novel mitogenic lectin was isolated. Purification was carried out by affinity chromatography on Sephadex G-100. The tetrameric lectin was a glycoprotein with a MW of 40,000; it consist of 2 large .beta.-subunits (MW 14,000) and 2 small .alpha.-subunits (MW 6000). The N-terminal sequence of both subunits and their amino acid compositions were determined. Lectin agglutinated human erythrocytes, preferring group B, and erythrocytes from rabbits and horses; no agglutination took place with sheep erythrocytes. Agglutination was inhibited by mono-, di- and tri-saccharides with the configuration of glucose at the free 4-hydroxyl group. Lectin stimulates mitosis in lymphocytes of mice. From the seeds of the same plant, a protein was isolated which binds to the lectin described above. The lectin binder consists of subunits with a MW of 53,500.