<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Adikane, H. V.</style></author><author><style face="normal" font="default" size="100%">Iyer, G. J.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Chemical modification of ethyl cellulose-based highly porous membrane for the purification of immunoglobulin G</style></title><secondary-title><style face="normal" font="default" size="100%">Applied Biochemistry and Biotechnology</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Affinity bioseparation</style></keyword><keyword><style  face="normal" font="default" size="100%">Ethyl cellulose</style></keyword><keyword><style  face="normal" font="default" size="100%">Glutaraldehyde</style></keyword><keyword><style  face="normal" font="default" size="100%">Immunoglobulin G</style></keyword><keyword><style  face="normal" font="default" size="100%">Polyethylenimine</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein A</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2013</style></year><pub-dates><date><style  face="normal" font="default" size="100%">FEB</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">3</style></number><publisher><style face="normal" font="default" size="100%">HUMANA PRESS INC</style></publisher><pub-location><style face="normal" font="default" size="100%">999 RIVERVIEW DRIVE SUITE 208, TOTOWA, NJ 07512 USA</style></pub-location><volume><style face="normal" font="default" size="100%">169</style></volume><pages><style face="normal" font="default" size="100%">1026-1038</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The chemical modification of developed ethyl cellulose-based membrane was carried out to make it suitable for bioseparation. The different reagents were used for the modification of membrane to couple protein A (PA) to study the purification of immunoglobulin G (IgG) from blood. The chemical modification was carried out using relatively simple and mild reaction conditions. The attenuated total reflectance Fourier transform infrared analysis of chemically modified membrane showed new peak at 1,596.06 and 1,716.49 cm(-1). The scanning electron microscopy of PA-coupled membrane, which was used for IgG purification showed open pores and 950 +/- 21.5 LMH (L m(-2) h(-1)) operational flux at 0.5-bar out pressure. The flux of unmodified membrane was 1,746 +/- 18.5 LMH at 0.5-bar out pressure. The equilibrium adsorption concentration (318.5 +/- 5.9 mu g cm(-2)) was obtained at 3 h. The adsorption character of PA-coupled membrane was consistent with the Langmuir adsorption model and the non-specific binding was 67.08 +/- 1.3 mu g cm(-2). The sodium dodecyl sulfate polyacrylamide gel electrophoresis analysis showed similar purification pattern for purified IgG from human serum and commercial preparation of IgG. All the results have suggested a high potential of PA-coupled ethyl cellulose-based membrane for large-scale purification of IgG.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">3</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">1.687
</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Amritkar, Vinod</style></author><author><style face="normal" font="default" size="100%">Adat, Satish</style></author><author><style face="normal" font="default" size="100%">Tejwani, Vijay</style></author><author><style face="normal" font="default" size="100%">Rathore, Anurag</style></author><author><style face="normal" font="default" size="100%">Bhambure, Rahul</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Engineering staphylococcal protein A for high-throughput affinity purification of monoclonal antibodies</style></title><secondary-title><style face="normal" font="default" size="100%">Biotechnology Advances</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Alkaline tolerance</style></keyword><keyword><style  face="normal" font="default" size="100%">Dynamic binding capacity</style></keyword><keyword><style  face="normal" font="default" size="100%">Elution pH</style></keyword><keyword><style  face="normal" font="default" size="100%">Monoclonal antibodies</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein A</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2020</style></year><pub-dates><date><style  face="normal" font="default" size="100%">NOV </style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">44</style></volume><pages><style face="normal" font="default" size="100%">107632</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Protein A chromatography is one of the most widely used purification steps in the manufacturing of the various classes of recombinant and non-recombinant antibodies. Due to the higher cost, lower binding capacity, and limited life cycle of Protein A ligand, this affinity-based purification step is often one of the most significant contributors to the cost of manufacturing of monoclonal antibody (mAb) products. In the last decade, there has been significant progress in improving the Protein A chromatography throughput by designing new engineered Staphylococcal Protein A (SPA) variants with higher dynamic binding capacity, considerable alkaline tolerance, and mild acidic elution pH. This review aims at summarizing the various protein engineering approaches used for improving the throughput of the Protein A-based affinity purification of various immunoglobulins. With biopharmaceutical producers operating under ever-increasing pressure towards reducing the cost of manufacturing, these advances in engineered protein A variants will help in processing larger cell culture volumes with high throughput and thereby significantly lower the cost of raw materials.&lt;/p&gt;
</style></abstract><work-type><style face="normal" font="default" size="100%">Review</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;Foreign&lt;/p&gt;
</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;10.744&lt;/p&gt;
</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Deulgaonkar, Prashant</style></author><author><style face="normal" font="default" size="100%">Bhambure, Rahul</style></author><author><style face="normal" font="default" size="100%">Prasad, Bhaskarjyoti</style></author><author><style face="normal" font="default" size="100%">Mishra, Ashok</style></author><author><style face="normal" font="default" size="100%">Tiwari, Sanjay</style></author><author><style face="normal" font="default" size="100%">Mody, Rustom</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Mechanistic modeling of continuous capture step purification of biosimilar monoclonal antibody therapeutic</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Chemical Technology and Biotechnology</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">CaptureSMB</style></keyword><keyword><style  face="normal" font="default" size="100%">continuous chromatography</style></keyword><keyword><style  face="normal" font="default" size="100%">Mathematical modeling</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein A</style></keyword><keyword><style  face="normal" font="default" size="100%">simulation</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2022</style></year><pub-dates><date><style  face="normal" font="default" size="100%">SEP</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">97</style></volume><pages><style face="normal" font="default" size="100%">2404-2419</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	{BACKGROUND Continuous multicolumn Protein A chromatography offers various advantages for capture stage purification of monoclonal antibody therapeutics, like higher productivity and resin capacity utilization, lower buffer consumption, small footprint, etc. Due to the complexity of the continuous process, experimental optimization is time-consuming and cost-intensive. This investigation proposes a hybrid process development approach integrating experimental and mechanistic modeling for time- and cost-effective development and optimization of continuous Protein A affinity chromatography. RESULTS Productivity and capacity utilization of the continuous CaptureSMB process under varying operating conditions were predicted using the Chromatography Analysis and Design Toolkit (CADET) framework and validated with experimental results. Effects of critical process parameters like feed concentration (c(0)), loading breakthrough (s) and residence time (RT) on productivity and capacity utilization were evaluated. Model predictions were validated using the experimental results proving the reliability and feasibility of the modeling approach. At 15.00 +/- 0.20 mg mL(-1) feed model mAb concentration, the model-based approach predicted the best performance giving 27.56 g L-1 h(-1) productivity (RT = 2 min&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">9</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;
	Foreign&lt;/p&gt;
</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;
	3.709&lt;/p&gt;
</style></custom4></record></records></xml>