Practical Protein Chemistry - A. Darbre 1989
Affinity Chromatography of Proteins
General Procedures in Affinity Chromatography
Immobilized Lectins
If purified preparations of highly specific ligands are unavailable, general Affinity Chromatography techniques based on group-specific ligands are employed. Currently, Three types of affinity sorbents are most widely used:
1) immobilized Lectins for isolating soluble or Cell wall-incorporated Glycoproteins;
2) Immobilized Antibodies for obtaining purified antigen preparations;
3) immobilized enzyme Cofactors.
Chromatography using immobilized lectins relies on their selective affinity for various terminal CARBOHYDRATES or carbohydrate groups within the glycoprotein molecule. Immobilized concanavalin A or lentil lectin is used for the specific isolation of glycoproteins or Cells containing glucose or mannose residues. Immobilized limulin is employed to isolate glycoproteins with a high sialic acid content. Immobilized peanut agglutinin exhibits Specificity toward glycoproteins containing N-acetylgalactosamine, as well as toward T-lymphocyte populations at various stages of differentiation. Elution is performed using concentrated carbohydrate solutions with the appropriate specificity for the given lectin. For example, α-glucopyranoside is used for elution from immobilized concanavalin A or lentil lectin, whereas sialic acids are used in the case of immobilized limulin.
Last update: 06/08/2026
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