Three lectins have been isolated from an extract of mistletoe (Viscum album) by affinity chromatography on partially hydrolysed Sepharose and human immunoglobulin- Sepharose. The lectins differ in molecular weight and sugar specificity (lectin I, mol.wt. 11500, D-galactose-specific; lectin II, mol.wt. 60000, both D-galactose- and N-acetyl-D-galactosamine-specific; lectin III, mol. wt. 50000, N-acetyl-D-galactosamine-specific). All three lectins react with human erythrocytes without specificity for the A, B, and O blood groups. In contrast with abrin and ricin the mistletoe lectins cannot be divided into "toxins" and "haemagglutinins".
A lectin from Viscum album which specifically binds to D-galactose was isolated by affinity chromatography on O-lactosyl-, O-galactosyl-polycarylamide or hydrolized sepharose 4 B. Some serological and physicochemical properties of the agglutination are reported.
Molecules of mistletoe lectin I (ML I) were investigated electron microscopically by negative staining with uranyl salts. An equilibrium was found between monomers and dimers at the used protein concentration. ML I monomers show a nearly triangular or rounded profile with dimensions of 80 × 90 Å. ML I dimers are rod‐like particles composed of two triangular parts which are dislocated against each other. In another view the dimers appear thinner without a pronounced substructure. The dimensions of the dimers are 175 × 80 × 60 Å.
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