#CAPTO MMC IMPRES SERIES#

The second experimental series studied the impact of phase modifiers, ethylene glycol, urea, and arginine on the mixed mode mediated removal.

Both single mode anion exchange and hydrophobic interaction resins failed to separate LHF. The first experimental series consisted of comparison to chromatographic behavior on corresponding single mode resins. The mechanism of fragment removal was investigated in two series of experiments. Removal of greater than 75% of LHF population occurred at pH 8 and low conductivity. Capto adhere, HEA Hypercel, and PPA Hypercel anion exchange/hydrophobic interaction mixed mode resins were evaluated for their fragment removal capabilities and found to separate large hinge IgG1 antibody fragment (LHF) from monomer. Biophys Chem 127:1–8īurgess RR (2018) A brief practical review of size exclusion chromatography: rules of thumb, limitations, and troubleshooting.Efforts to increase monoclonal antibody expression in cell culture can result in the presence of fragmented species requiring removal in downstream processing. Data file 29-0356-74 ABĪrakawa T, Ejima D, Tsumoto K, Obeyama N, Tanaka Y, Kita Y, Timasheff SN (2007) Suppression of protein interactions by arginine: a proposed mechanism of the arginine effects. GE Healthcare Life Sciences (2015) Capto™ MMC ImpRes. GE Healthcare Life Sciences (2013) Polishing of monoclonal antibodies using Capto™ MMC ImpRes in bind and elute mode. J Chromatogr A 1294:70–75Ĭhmielowski RA, Meissner S, Roush D, Linden TO, Glowacki E, Konietzko J, Nti-Gyabaah J (2014) Resolution of heterogeneous charged antibody aggregates via multimodal chromatography: a comparison to conventional approaches. Gao D, Wang LL, Lin DQ, Yao SJ (2013) Evaluating antibody monomer separation from associated aggregates using mixed-mode chromatography. Bioprocess Int 7:52–56Ĭhen J, Tetrault J, Zhang Y, Wasserman A, Conley G, Dileo M, Haimes E, Nixon AE, Ley A (2010) The distinctive separation attributes of mixed-mode resins and their application in monoclonal antibody downstream purification process. Curr Pharm Biotechnol 10:440–446Įriksson K, Ljunglöf A, Rodrigo G, Brekkan E (2009) MAb contaminant removal with a multimodal anion exchanger: a platform step to follow protein A. Gagnon P, Beam K (2009) Antibody aggregate removal by hydroxyapatite chromatography.

Gagnon P, Ng P, Aberrin C, Zhen J, He J, Mekosh H, Cummings L, Richieri R, Zaidi S (2006) A ceramic hydroxyapatite based purification platform: simultaneous removal of leached protein A, aggregates, DNA, and endotoxins. McCue JT (2009) Theory and use of hydrophobic interaction chromatography in protein purification applications.

Lu Y, Williamson B, Gillespie R (2009) Recent advancement in application of hydrophobic interaction chromatography for aggregate removal in industrial purification process. McCue JT, Engel P, Ng A, Macniven R, Thömmes J (2008) Modeling of protein monomer/aggregate purification and separation using hydrophobic interaction chromatography. Zhang X, Chen T, Li Y (2019) A parallel demonstration of different resins' antibody aggregate removing capability by a case study. He X (2015) Mixed-mode chromatography for mAb S aggregate removal: comparison of CHT™ ceramic hydroxyapatite, capto adhere, and capto adhere impres. Hall T, Wilson JJ, Brownlee TJ, Swartling JR, Langan SE, Lambooy PK (2015) Alkaline cation-exchange chromatography for the reduction of aggregate and a mis-formed disulfide variant in a bispecific antibody purification process. Vázquez-Rey M, Lang DA (2011) Aggregates in monoclonal antibody manufacturing processes. Bonnerjea J, Brake RP, Davis MR, Kellerman K, Preneta A (2008) Ion exchange chromatography and purification of antibodies, United States patent application publication US 2008/0312425 A1

Capto mmc impres