Influence of type of linkage and spacer on the interaction of beta-galactoside-binding proteins with immobilized affinity ligands.

@article{Gabius1990InfluenceOT,
  title={Influence of type of linkage and spacer on the interaction of beta-galactoside-binding proteins with immobilized affinity ligands.},
  author={Hans Joachim Gabius},
  journal={Analytical biochemistry},
  year={1990},
  volume={189 1},
  pages={91-4}
}
Affinity chromatography provides a powerful tool for isolation of carbohydrate-binding proteins. However, the choice of the ligand and spacer has an important impact on effectiveness. The influence of several different ligands on qualitative and quantitative aspects of the purification of two beta-galactoside-specific lectins has been evaluated. Sepharose was modified by coupling four types of neoglycoproteins (galactosylated or lactosylated bovine serum albumin with increasing sugar content… CONTINUE READING

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