Static and dynamic binding behavior of an IgG2 monoclonal antibody with several new mixed mode affinity adsorbents

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Static and dynamic binding behavior of an IgG2 monoclonal antibody with several new mixed mode affinity adsorbents

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作者：Chih-Pei Lin ; Kei Saito ; Reinhard I. Boysen ; Eva M. Campi ; Milton T.W. Hearn ; ^{milton.hearn@monash.edu" class="auth_mail" title="E-mail the corresponding author}
关键词：c&lowast ; equilibrium binding concentration ; ci ; initial protein concentration ; HCP ; host cell protein ; Ka ; equilibrium binding constant ; mAb ; monoclonal antibody ; MEP ; 4-mercaptoethylpyridine ; PSEAs ; pyridinylsulfanylethylamines ; ν ; ratio of the volume of adsorbent to total volume of incubate ; q&lowast ; amount of protein per mL adsorbent bound at equilibrium ; qm ; maximum binding capacity ; terpy ; 4&prime ; -aminoethylsulfanyl-2 ; 2&prime ; 6&prime ; 2&Prime ; -terpyridine ; TIG ; terpy-immobilized gels
刊名：Separation and Purification Technology
出版年：2016
出版时间：11 May 2016
年：2016
卷：163
期：Complete
页码：199-205
全文大小：807 K

文摘

•: Several new mixed-mode ligand-based adsorbents have been investigated.
•: Selectivity for an IgG2 mAb is dependent on subtle changes in ligand structure.
•: Adsorption isotherms have been determined and m>K_am> and Qmax values derived.
•: Efficient recovery of IgG2 mAbs from crude cell culture harvests achieved.
•: Host cell protein clearance found to be influenced by the ligand structure.

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