IMMUNOGLOBULIN PURIFICATION BY AFFINITY CHROMATOGRAPHY USING PROTEIN A MIMETIC LIGANDS PREPARED BY COMBINATORIAL CHEMICAL SYNTHESIS

@article{Kabir2002IMMUNOGLOBULINPB,
  title={IMMUNOGLOBULIN PURIFICATION BY AFFINITY CHROMATOGRAPHY USING PROTEIN A MIMETIC LIGANDS PREPARED BY COMBINATORIAL CHEMICAL SYNTHESIS},
  author={Shahjahan Kabir},
  journal={Immunological Investigations},
  year={2002},
  volume={31},
  pages={263 - 278}
}
  • S. Kabir
  • Published 1 January 2002
  • Biology, Chemistry
  • Immunological Investigations
Affinity chromatography using protein A from Staphylococcus aureus as the ligand has been widely used for the isolation of immunoglobulin G (IgG) from various species. Since ligand leakage from the affinity support can occur, time consuming analytical controls are required to detect the presence of contaminants associated with the isolated IgG prior to its use for therapeutic purpose in humans. Besides, protein A is an expensive bacterial product, whose isolation involves complex and labor… 

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References

SHOWING 1-10 OF 58 REFERENCES

Affinity purification of immunoglobulin M using a novel synthetic ligand.

Protein a mimetic peptide ligand for affinity purification of antibodies

The tetrameric tripeptide identified after three screening cycles was produced in larger amounts and then immobilized in high yield on preactivated solid support for the preparation of affinity columns, which proved useful for a very convenient one‐step purification of antibodies directly from crude sera.

Affinity purification of mouse monoclonal IgE using a protein A mimetic ligand (TG19318) immobilized on solid supports

TG19318 affinity columns proved useful for a very convenient one‐step purification of IgE directly from crude ascites, as determined by immunoassays on antigen‐coated plates, and up to 5 mg of IgEs could be purified on a 1 ml column in a single run.

A preliminary study for isolation of catalytic antibodies by histidine ligand affinity chromatography as an alternative to conventional protein A/G methods

Catalytic autoimmune antibodies from the sera of lupus patients were purified using histidyl-aminohexyl-Sepharose gel and compared with the antibodies purified with protein A and protein G affinity chromatography, finding histidine affinity offer a superior method for isolating autoimmune catalytic antibodies.

A synthetic ligand for IgA affinity purification

TG19318, a synthetic ligand deduced from the screening of combinatorial libraries, displays specific and selective recognition properties for immunoglobulins of the G class and can be used conveniently for affinity chromatography purification of monoclonal and polyclonal antibodies.

Immunoglobulin specificity of TG19318: a novel synthetic ligand for antibody affinity purification

Validation of antibody affinity purification processes for therapeutic use is going to be simplified by the use of TG19318, which could reduce considerably the presence of biological contaminants in the purified preparation, a very recurrent problem when using recombinant or extractive biomolecules as affinity ligands.

A one-step purification of membrane proteins using a high efficiency immunomatrix.

A strategy for the generation of biomimetic ligands for affinity chromatography. Combinatorial synthesis and biological evaluation of an IgG binding ligand

An IgG‐binding ligand library comprising 88 adsorbents based on a known lead compound was generated on an agarose solid phase and it was found that ligands comprising 3‐aminophenol and an aminonaphthol moiety substiuted on a triazine nucleus generally performed better than other ligands in the library.

Design, synthesis, and application of a Protein A mimetic

A nonpeptidyl mimic for Staphylococcus aureus Protein A (SpA) is developed that binds IgG competitively with SpA in solution and when immobilized on agarose beads, with an affinity constant of 105-106 M−1.
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