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Journal ArticleDOI

Effective elution of antibodies by arginine and arginine derivatives in affinity column chromatography.

TLDR
Arginine was effective in eluting monoclonal antibodies IgG1 and IgG4 and effective in fractionation of pAbs using antigen-conjugated affinity columns, and GdnHCl was also effective under similar conditions, but the eluted material showed more aggregation than did the protein eluted by arginine.
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This article is published in Analytical Biochemistry.The article was published on 2005-10-15. It has received 131 citations till now. The article focuses on the topics: Arginine & Guanidine.

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Citations
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Journal ArticleDOI

Protein aggregation and bioprocessing.

TL;DR: Care should be taken when developing a process to monitor the compatibility of the equipment and process with the protein to ensure that potential aggregation is minimized and steps to remove aggregates have been successfully used at a manufacturing scale.
Journal ArticleDOI

Suppression of protein interactions by arginine: a proposed mechanism of the arginine effects.

TL;DR: While arginine increases the surface tension of water, it favorably interacts with most amino acid side chains and the peptide bonds, a property shared with GdnHCl.
Journal ArticleDOI

Technology trends in antibody purification.

TL;DR: Technology trends in antibody purification are reviewed, including recent innovations in size exclusion, anion exchange, cation exchange, hydrophobic interaction, immobilized metal affinity, mixed-mode, and bioaffinity chromatography.
Journal ArticleDOI

Biotechnology applications of amino acids in protein purification and formulations.

TL;DR: This review covers various biotechnology applications of amino acids, in particular arginine, which finds much wider applications than previously anticipated in the research and development of proteins, in particularly in pharmaceutical applications.
Journal ArticleDOI

The critical role of mobile phase composition in size exclusion chromatography of protein pharmaceuticals.

TL;DR: The role that addition of various cosolvents to the mobile phase plays in suppressing that protein adsorption to the resin is focused on.
References
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Book ChapterDOI

[31] Affinity chromatography

TL;DR: Inherent advantages of this method of purification are the rapidity and ease of a potentially single-step procedure, the rapid separation of the protein to be purified from inhibitors and destructive contaminants, such as proteases, and protection from denaturation during purification by active site ligand-stabilization of protein tertiary structure.
Journal ArticleDOI

The Thermal Stability of Immunoglobulin: Unfolding and Aggregation of a Multi-Domain Protein

TL;DR: A strong correlation exists between the denaturation transitions as observed by calorimetry and the changes in secondary structure derived from circular dichroism, after both heat- and low-pH-induced denaturation, a significant fraction of the secondary structure remains.
Journal ArticleDOI

Mechanism of protein salting in and salting out by divalent cation salts: balance between hydration and salt binding.

TL;DR: It was shown that the binding of divalent cations to the proteins overcomes the salt exclusion due to the surface tension increase, leading to a decrease in the preferential hydration, supported by a strong correlation between the preferential interaction results and the interaction of these salts with the model peptide compound acetyltetraglycine ethyl ester.
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