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Ganesh Vedantham - One of the best experts on this subject based on the ideXlab platform.
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caprylic Acid Precipitation method for impurity reduction an alternative to conventional chromatography for monoclonal antibody purification
Biotechnology and Bioengineering, 2012Co-Authors: Yan Brodsky, Yinges Yigzaw, Cheng Zhang, Ganesh VedanthamAbstract:We report the use of caprylic Acid based impurity Precipitation as (1) an alternative method to polishing chromatography techniques commonly used for monoclonal antibody purification and (2) an impurity reduction step prior to harvesting the bioreactor. This impurity reduction method was tested with protein A purified antibodies and with cell culture fluid. First, the operational parameters influencing Precipitation of host cell proteins and high molecular weight aggregate in protein A pools were investigated. When used as a polishing step, the primary factor affecting purification and yield was determined to be pH. Caprylic Acid Precipitation was comparable to polishing IEX chromatography in reducing host cell protein and aggregate levels. A virus reduction study showed complete clearance of a model retrovirus during caprylic Acid Precipitation of protein A purified antibody. Caprylic Acid mediated impurity Precipitation in cell culture showed that the impurity clearance was generally insensitive to pH and caprylic Acid concentration whereas yield was a function of caprylic Acid concentration. Protein A purification of caprylic Acid precipitated cell culture fluid generated less turbid product pool with reduced levels of host cell proteins and high molecular weight aggregate. The results of this study show caprylic Acid Precipitation to be an effective purification method that can be incorporated into a production facility with minimal cost as it utilizes existing tanks and process flow. Eliminating flow through chromatography polishing step can provide process intensification by avoiding the process tank volume constraints for high titer processes. Biotechnol. Bioeng. 2012; 109: 2589–2598. © 2012 Wiley Periodicals, Inc.
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caprylic Acid Precipitation method for impurity reduction an alternative to conventional chromatography for monoclonal antibody purification
Biotechnology and Bioengineering, 2012Co-Authors: Yan Brodsky, Yinges Yigzaw, Cheng Zhang, Ganesh VedanthamAbstract:We report the use of caprylic Acid based impurity Precipitation as (1) an alternative method to polishing chromatography techniques commonly used for monoclonal antibody purification and (2) an impurity reduction step prior to harvesting the bioreactor. This impurity reduction method was tested with protein A purified antibodies and with cell culture fluid. First, the operational parameters influencing Precipitation of host cell proteins and high molecular weight aggregate in protein A pools were investigated. When used as a polishing step, the primary factor affecting purification and yield was determined to be pH. Caprylic Acid Precipitation was comparable to polishing IEX chromatography in reducing host cell protein and aggregate levels. A virus reduction study showed complete clearance of a model retrovirus during caprylic Acid Precipitation of protein A purified antibody. Caprylic Acid mediated impurity Precipitation in cell culture showed that the impurity clearance was generally insensitive to pH and caprylic Acid concentration whereas yield was a function of caprylic Acid concentration. Protein A purification of caprylic Acid precipitated cell culture fluid generated less turbid product pool with reduced levels of host cell proteins and high molecular weight aggregate. The results of this study show caprylic Acid Precipitation to be an effective purification method that can be incorporated into a production facility with minimal cost as it utilizes existing tanks and process flow. Eliminating flow through chromatography polishing step can provide process intensification by avoiding the process tank volume constraints for high titer processes.
Yan Brodsky - One of the best experts on this subject based on the ideXlab platform.
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caprylic Acid Precipitation method for impurity reduction an alternative to conventional chromatography for monoclonal antibody purification
Biotechnology and Bioengineering, 2012Co-Authors: Yan Brodsky, Yinges Yigzaw, Cheng Zhang, Ganesh VedanthamAbstract:We report the use of caprylic Acid based impurity Precipitation as (1) an alternative method to polishing chromatography techniques commonly used for monoclonal antibody purification and (2) an impurity reduction step prior to harvesting the bioreactor. This impurity reduction method was tested with protein A purified antibodies and with cell culture fluid. First, the operational parameters influencing Precipitation of host cell proteins and high molecular weight aggregate in protein A pools were investigated. When used as a polishing step, the primary factor affecting purification and yield was determined to be pH. Caprylic Acid Precipitation was comparable to polishing IEX chromatography in reducing host cell protein and aggregate levels. A virus reduction study showed complete clearance of a model retrovirus during caprylic Acid Precipitation of protein A purified antibody. Caprylic Acid mediated impurity Precipitation in cell culture showed that the impurity clearance was generally insensitive to pH and caprylic Acid concentration whereas yield was a function of caprylic Acid concentration. Protein A purification of caprylic Acid precipitated cell culture fluid generated less turbid product pool with reduced levels of host cell proteins and high molecular weight aggregate. The results of this study show caprylic Acid Precipitation to be an effective purification method that can be incorporated into a production facility with minimal cost as it utilizes existing tanks and process flow. Eliminating flow through chromatography polishing step can provide process intensification by avoiding the process tank volume constraints for high titer processes. Biotechnol. Bioeng. 2012; 109: 2589–2598. © 2012 Wiley Periodicals, Inc.
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caprylic Acid Precipitation method for impurity reduction an alternative to conventional chromatography for monoclonal antibody purification
Biotechnology and Bioengineering, 2012Co-Authors: Yan Brodsky, Yinges Yigzaw, Cheng Zhang, Ganesh VedanthamAbstract:We report the use of caprylic Acid based impurity Precipitation as (1) an alternative method to polishing chromatography techniques commonly used for monoclonal antibody purification and (2) an impurity reduction step prior to harvesting the bioreactor. This impurity reduction method was tested with protein A purified antibodies and with cell culture fluid. First, the operational parameters influencing Precipitation of host cell proteins and high molecular weight aggregate in protein A pools were investigated. When used as a polishing step, the primary factor affecting purification and yield was determined to be pH. Caprylic Acid Precipitation was comparable to polishing IEX chromatography in reducing host cell protein and aggregate levels. A virus reduction study showed complete clearance of a model retrovirus during caprylic Acid Precipitation of protein A purified antibody. Caprylic Acid mediated impurity Precipitation in cell culture showed that the impurity clearance was generally insensitive to pH and caprylic Acid concentration whereas yield was a function of caprylic Acid concentration. Protein A purification of caprylic Acid precipitated cell culture fluid generated less turbid product pool with reduced levels of host cell proteins and high molecular weight aggregate. The results of this study show caprylic Acid Precipitation to be an effective purification method that can be incorporated into a production facility with minimal cost as it utilizes existing tanks and process flow. Eliminating flow through chromatography polishing step can provide process intensification by avoiding the process tank volume constraints for high titer processes.
Cheng Zhang - One of the best experts on this subject based on the ideXlab platform.
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caprylic Acid Precipitation method for impurity reduction an alternative to conventional chromatography for monoclonal antibody purification
Biotechnology and Bioengineering, 2012Co-Authors: Yan Brodsky, Yinges Yigzaw, Cheng Zhang, Ganesh VedanthamAbstract:We report the use of caprylic Acid based impurity Precipitation as (1) an alternative method to polishing chromatography techniques commonly used for monoclonal antibody purification and (2) an impurity reduction step prior to harvesting the bioreactor. This impurity reduction method was tested with protein A purified antibodies and with cell culture fluid. First, the operational parameters influencing Precipitation of host cell proteins and high molecular weight aggregate in protein A pools were investigated. When used as a polishing step, the primary factor affecting purification and yield was determined to be pH. Caprylic Acid Precipitation was comparable to polishing IEX chromatography in reducing host cell protein and aggregate levels. A virus reduction study showed complete clearance of a model retrovirus during caprylic Acid Precipitation of protein A purified antibody. Caprylic Acid mediated impurity Precipitation in cell culture showed that the impurity clearance was generally insensitive to pH and caprylic Acid concentration whereas yield was a function of caprylic Acid concentration. Protein A purification of caprylic Acid precipitated cell culture fluid generated less turbid product pool with reduced levels of host cell proteins and high molecular weight aggregate. The results of this study show caprylic Acid Precipitation to be an effective purification method that can be incorporated into a production facility with minimal cost as it utilizes existing tanks and process flow. Eliminating flow through chromatography polishing step can provide process intensification by avoiding the process tank volume constraints for high titer processes. Biotechnol. Bioeng. 2012; 109: 2589–2598. © 2012 Wiley Periodicals, Inc.
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caprylic Acid Precipitation method for impurity reduction an alternative to conventional chromatography for monoclonal antibody purification
Biotechnology and Bioengineering, 2012Co-Authors: Yan Brodsky, Yinges Yigzaw, Cheng Zhang, Ganesh VedanthamAbstract:We report the use of caprylic Acid based impurity Precipitation as (1) an alternative method to polishing chromatography techniques commonly used for monoclonal antibody purification and (2) an impurity reduction step prior to harvesting the bioreactor. This impurity reduction method was tested with protein A purified antibodies and with cell culture fluid. First, the operational parameters influencing Precipitation of host cell proteins and high molecular weight aggregate in protein A pools were investigated. When used as a polishing step, the primary factor affecting purification and yield was determined to be pH. Caprylic Acid Precipitation was comparable to polishing IEX chromatography in reducing host cell protein and aggregate levels. A virus reduction study showed complete clearance of a model retrovirus during caprylic Acid Precipitation of protein A purified antibody. Caprylic Acid mediated impurity Precipitation in cell culture showed that the impurity clearance was generally insensitive to pH and caprylic Acid concentration whereas yield was a function of caprylic Acid concentration. Protein A purification of caprylic Acid precipitated cell culture fluid generated less turbid product pool with reduced levels of host cell proteins and high molecular weight aggregate. The results of this study show caprylic Acid Precipitation to be an effective purification method that can be incorporated into a production facility with minimal cost as it utilizes existing tanks and process flow. Eliminating flow through chromatography polishing step can provide process intensification by avoiding the process tank volume constraints for high titer processes.
Yinges Yigzaw - One of the best experts on this subject based on the ideXlab platform.
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caprylic Acid Precipitation method for impurity reduction an alternative to conventional chromatography for monoclonal antibody purification
Biotechnology and Bioengineering, 2012Co-Authors: Yan Brodsky, Yinges Yigzaw, Cheng Zhang, Ganesh VedanthamAbstract:We report the use of caprylic Acid based impurity Precipitation as (1) an alternative method to polishing chromatography techniques commonly used for monoclonal antibody purification and (2) an impurity reduction step prior to harvesting the bioreactor. This impurity reduction method was tested with protein A purified antibodies and with cell culture fluid. First, the operational parameters influencing Precipitation of host cell proteins and high molecular weight aggregate in protein A pools were investigated. When used as a polishing step, the primary factor affecting purification and yield was determined to be pH. Caprylic Acid Precipitation was comparable to polishing IEX chromatography in reducing host cell protein and aggregate levels. A virus reduction study showed complete clearance of a model retrovirus during caprylic Acid Precipitation of protein A purified antibody. Caprylic Acid mediated impurity Precipitation in cell culture showed that the impurity clearance was generally insensitive to pH and caprylic Acid concentration whereas yield was a function of caprylic Acid concentration. Protein A purification of caprylic Acid precipitated cell culture fluid generated less turbid product pool with reduced levels of host cell proteins and high molecular weight aggregate. The results of this study show caprylic Acid Precipitation to be an effective purification method that can be incorporated into a production facility with minimal cost as it utilizes existing tanks and process flow. Eliminating flow through chromatography polishing step can provide process intensification by avoiding the process tank volume constraints for high titer processes. Biotechnol. Bioeng. 2012; 109: 2589–2598. © 2012 Wiley Periodicals, Inc.
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caprylic Acid Precipitation method for impurity reduction an alternative to conventional chromatography for monoclonal antibody purification
Biotechnology and Bioengineering, 2012Co-Authors: Yan Brodsky, Yinges Yigzaw, Cheng Zhang, Ganesh VedanthamAbstract:We report the use of caprylic Acid based impurity Precipitation as (1) an alternative method to polishing chromatography techniques commonly used for monoclonal antibody purification and (2) an impurity reduction step prior to harvesting the bioreactor. This impurity reduction method was tested with protein A purified antibodies and with cell culture fluid. First, the operational parameters influencing Precipitation of host cell proteins and high molecular weight aggregate in protein A pools were investigated. When used as a polishing step, the primary factor affecting purification and yield was determined to be pH. Caprylic Acid Precipitation was comparable to polishing IEX chromatography in reducing host cell protein and aggregate levels. A virus reduction study showed complete clearance of a model retrovirus during caprylic Acid Precipitation of protein A purified antibody. Caprylic Acid mediated impurity Precipitation in cell culture showed that the impurity clearance was generally insensitive to pH and caprylic Acid concentration whereas yield was a function of caprylic Acid concentration. Protein A purification of caprylic Acid precipitated cell culture fluid generated less turbid product pool with reduced levels of host cell proteins and high molecular weight aggregate. The results of this study show caprylic Acid Precipitation to be an effective purification method that can be incorporated into a production facility with minimal cost as it utilizes existing tanks and process flow. Eliminating flow through chromatography polishing step can provide process intensification by avoiding the process tank volume constraints for high titer processes.
Rui Nian - One of the best experts on this subject based on the ideXlab platform.
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reduction of chromatin heteroaggregates by Acid Precipitation of mammalian cell culture and ramification in protein a chromatography for recombinant immunoglobulin g purification
Biochemical Engineering Journal, 2019Co-Authors: Wenshuai Liu, Quan Chen, Yue Sun, Mo Xian, Dongyan Zhou, Zixian Bao, Xiying Fan, Yunlong Liang, Xinying Peng, Rui NianAbstract:Abstract Acid Precipitation has been demonstrated as a clarification method for cell culture supernatant (CCS) pretreatment during Immunoglobulin G (IgG) purification. In this study, the responses of IgG, non-histone host cell protein (n-hHCP), histone, and DNA to different pHs in the presence of salt (NaCl) at various concentrations were systematically studied. IgG loss was closely associated with the Precipitation of chromatin heteroaggregates, in which DNA/histone showed significant decreases along with the Acidification of buffer environment. In addition, DNA showed full recovery after pH neutralization, while the low pH treatment induced histone Precipitation was permanent and could not be reverted upon pH increase. Analytical size exclusion chromatography (SEC) profiles further indicated the agglomeration and reduction of chromatin heteroaggregates along with lower pH. Protein A chromatography benefited from the reduction of chromatin heteroaggregates and showed significant enhancement of the removal of impurities as well as for IgG recovery. For the first time, this study correlated CCS Acidification with chromatin heteroaggregate removal and illustrated its ramification for the subsequent purification process.
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histone dependent igg conservation in octanoic Acid Precipitation and its mechanism
Applied Microbiology and Biotechnology, 2016Co-Authors: Quan Chen, Phyllicia Toh, Yue Sun, Sarah Maria Abdul Latiff, Aina Hoi, Mo Xian, Haibo Zhang, Rui Nian, Wei Zhang, Pete GagnonAbstract:Octanoic Acid (OA) Precipitation has long been used in protein purification. Recently, we reported a new cell culture clarification method for immunoglobulin G (IgG) purification, employing an advance elimination of chromatin heteroaggregates with a hybrid OA-solid phase system. This treatment reduced DNA more than 3 logs, histone below the detection limit (LOD), and non-histone host cell proteins (nh-HCP) by 90 % while conserving more than 90 % of the IgG monomer. In this study, we further investigated the conservation of IgG monomer and antibody light chain (LC) to the addition of OA/OA-solid phase complex, with or without histone and DNA in different combinations. The results showed that highly basic histone protein was the prime target in OA/OA-solid phase Precipitation system for IgG purification, and the selective conservation of IgG monomer in this system was histone dependent. Our findings partially support the idea that OA works by sticking to electropositive hydrophobic domains on proteins, reducing their solubility, and causing them to agglomerate into large particles that precipitate from solution. Our findings also provide a new perspective for IgG purification and emphasize the necessity to re-examine the roles of various host contaminants in IgG purification.
