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Monovalent lectins, with only one binding site for carbohydrates, are usually not detectable
by agglutination assays. Therefore, agglutination assays are mostly applied for lectins that
are know to have more than one carbohydrate-binding site. Advances in biophysical and
molecular biology techniques as well as the availability of synthetic oligosaccharides have
contributed to the identification of many lectins. Most lectins have been purified by affinity
chromatography (Agrawal and Goldstein, 1967).
For the isolation and characterization of a vast number of lectins, sugarbased polymers like
Sephadex (glucose), Sepharose (galactose) or Chitin (N-acetyl-glucosamine) have been used.
Glycoproteinlinked matrices are applied to the purification of lectins that recognize more
complex saccharides (Goldstein, 2002). Many lectins have, in addition to the carbohydrate-
binding domain, another domain with distinct activity. Proteins that carry lectin domain(s)
and other domains with quite different properties have been better studied in animals than
in plants (Gabius, 1994).