![]() ![]() Original Assignee Bio Rad Laboratories Inc Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.) Gagnon Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.) Active Application number US12/422,141 Other versions US20090247735A1 Google Patents Enhanced capacity and purification of protein by mixed mode chromatography in the presence of aqueous-soluble nonionic organic polymersÄownload PDF Info Publication number US7999085B2 US7999085B2 US12/422,141 US42214109A US7999085B2 US 7999085 B2 US7999085 B2 US 7999085B2 US 42214109 A US42214109 A US 42214109A US 7999085 B2 US7999085 B2 US 7999085B2 Authority US United States Prior art keywords protein antibody target protein support mixed mode Prior art date Legal status (The legal status is an assumption and is not a legal conclusion. ![]() Google Patents US7999085B2 - Enhanced capacity and purification of protein by mixed mode chromatography in the presence of aqueous-soluble nonionic organic polymers However, additional affinities contributed by hydrophobic interaction or hydrogen bonding were also observed to play a role in the interaction between arginine and Capto MMC, which likely results in the characteristic elution by arginine.US7999085B2 - Enhanced capacity and purification of protein by mixed mode chromatography in the presence of aqueous-soluble nonionic organic polymers The overall affinity of arginine for Capto MMC was associated with electrostatic interactions. The mechanism of the effects of arginine on protein elution was determined by calculating the binding free energy between arginine and Capto MMC using molecular dynamics simulations. The purification of mAb-IL8 was successfully achieved using Capto MMC chromatography and arginine as the eluent. The effectiveness of arginine as an eluent also enabled the separation of monomeric BSA from the oligomeric forms. Arginine provides high recovery of monomeric BSA from Capto MMC chromatography columns at yields similar to NaCl elution, and oligomeric BSA was more readily eluted by arginine than by NaCl. 58-66 ISSN: 0021-9673 Subject: Gibbs free energy, arginine, bovine serum albumin, cations, chromatography, electrostatic interactions, hydrogen bonding, hydrophobic bonding, interleukin-8, molecular dynamics, monoclonal antibodies, simulation models, sodium chloride Abstract: This study highlights the ability of arginine to elute bovine serum albumin (BSA) and a monoclonal antibody against interleukin-8 (mAb-IL8) from Capto MMC, which is a multimodal cation exchanger. Interaction of arginine with Capto MMC in multimodal chromatography Author: Atsushi Hirano, Tsutomu Arakawa, Tomoshi Kameda Source: Journal of chromatography 2014 v.1338 pp.
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