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Related Experiment Videos

Histidine ligand affinity chromatography

M A Vijayalakshmi1

  • 1Laboratoire d'Intéractions Moléculaires et de Technologie des Séparations, University of Technology at Compiègne, France.

Molecular Biotechnology
|December 1, 1996
PubMed
Summary

Histidine immobilized sorbents offer a versatile pseudo-affinity purification method for diverse proteins. These adsorbents also enable simultaneous pyrogen removal and recovery of valuable blood proteins.

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Preparative biochemistry & biotechnology·2020

Area of Science:

  • Biochemistry
  • Separation Science
  • Biotechnology

Background:

  • Affinity chromatography is crucial for protein purification.
  • Developing broadly applicable and cost-effective ligands is essential.
  • Histidine offers a unique pseudo-affinity interaction for protein binding.

Purpose of the Study:

  • To describe sorbents with immobilized histidine as a versatile pseudo-affinity ligand.
  • To explore different support matrices for histidine immobilization.
  • To detail applications in protein purification and pyrogen removal.

Main Methods:

  • Immobilization of histidine onto various support matrices (particulate, membranes).
  • Characterization of sorbent specificity and binding mechanisms.
  • Development of protocols for protein purification and pyrogen removal.

Main Results:

  • Histidine-based sorbents demonstrate broad specificity for protein purification.
  • Both particulate and membrane supports are viable for histidine immobilization.
  • Effective protocols for scaled-up and scaled-down operations were established.
  • Simultaneous pyrogen removal and recovery of high-value blood proteins were achieved.

Conclusions:

  • Immobilized histidine is a highly effective pseudo-affinity ligand for diverse protein purification.
  • Histidine sorbents provide a flexible platform for various separation challenges, including pyrogen removal.
  • The described methods offer practical solutions for efficient and simultaneous purification and recovery processes.

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