Factorial screening of antibody purification processes using three chromatography steps without protein A

被引:170
作者
Follman, DK [1 ]
Farner, RL [1 ]
机构
[1] Genentech Inc, Dept Recovery Sci, San Francisco, CA 94080 USA
关键词
mixed-mode chromatography; factorial screening; antibodies;
D O I
10.1016/j.chroma.2003.10.060
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Protein A affinity chromatography is often employed as a capture step to meet the purity, yield, and throughput requirements for pharmaceutical antibody purification. However, a trade-off exists between step performance and price. Protein A resin removes 99.9% of feed stream impurities; however, its price is significantly greater than those of non-affinity media. With many therapeutic indications for antibodies requiring high doses and/or chronic administration, the consideration of process economics is critical. We have systematically evaluated the purification performance of cation-exchange, anion-exchange, hydroxyapatite, hydrophobic interaction, hydrophobic charge induction, and small-molecule ligand resins in each step of a three-step chromatographic purification process for a CHO-derived monoclonal antibody. Host cell proteins were removed to less-than-detectable for three processes (cation-exchange-anion-exchange-hydrophobic interaction chromatography, cation-exchange-anion-exchange-mixed cation-exchange chromatography, and cation-exchange-mixed cation-exchange-anion-exchange chromatography). The order of the process steps affected purification performance significantly. (C) 2003 Elsevier B.V. All rights reserved.
引用
收藏
页码:79 / 85
页数:7
相关论文
共 32 条
[1]   Targeted anti-cancer therapy using rituximab, a chimaeric anti-CD20 antibody (IDEC-C2B8) in the treatment of non-Hodgkin's B-cell lymphoma [J].
Anderson, DR ;
GrilloLopez, A ;
Varns, C ;
Chambers, KS ;
Hanna, N .
BIOCHEMICAL SOCIETY TRANSACTIONS, 1997, 25 (02) :705-708
[2]   Phase II study of weekly intravenous recombinant humanized Anti-p185(HER2) monoclonal antibody in patients with HER2/neu-overexpressing metastatic breast [J].
Baselga, J ;
Tripathy, D ;
Mendelsohn, J ;
Baughman, S ;
Benz, CC ;
Dantis, L ;
Sklarin, NT ;
Seidman, AD ;
Hudis, CA ;
Moore, J ;
Rosen, PP ;
Twaddell, T ;
Henderson, IC ;
Norton, L .
JOURNAL OF CLINICAL ONCOLOGY, 1996, 14 (03) :737-744
[3]   Expanded bed adsorption in the purification of monoclonal antibodies: a comparison of process alternatives [J].
Blank, GS ;
Zapata, G ;
Fahrner, R ;
Milton, M ;
Yedinak, C ;
Knudsen, H ;
Schmelzer, C .
BIOSEPARATION, 2001, 10 (1-3) :65-71
[4]  
Bodey B, 1996, ANTICANCER RES, V16, P517
[5]   Performance of a novel viresolve NFR virus filter [J].
Brough, H ;
Antoniou, C ;
Carter, J ;
Jakubik, J ;
Xu, Y ;
Lutz, H .
BIOTECHNOLOGY PROGRESS, 2002, 18 (04) :782-795
[6]   Results of 3-year phase III clinical trials with daclizumab prophylaxis for prevention of acute rejection after renal transplantation. [J].
Bumgardner, GL ;
Hardie, I ;
Johnson, RWG ;
Lin, A ;
Nashan, B ;
Pescovitz, MD ;
Ramos, E ;
Vincenti, F .
TRANSPLANTATION, 2001, 72 (05) :839-845
[7]   HUMANIZATION OF AN ANTI-P185HER2 ANTIBODY FOR HUMAN CANCER-THERAPY [J].
CARTER, P ;
PRESTA, L ;
GORMAN, CM ;
RIDGWAY, JBB ;
HENNER, D ;
WONG, WLT ;
ROWLAND, AM ;
KOTTS, C ;
CARVER, ME ;
SHEPARD, HM .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1992, 89 (10) :4285-4289
[8]  
CHEN AB, 1996, J BIOTECHNOL HEALTHC, V3, P70
[9]   SIZE-EXCLUSION REMOVAL OF MODEL MAMMALIAN VIRUSES USING A UNIQUE MEMBRANE SYSTEM .1. MEMBRANE QUALIFICATION [J].
DILEO, AJ ;
VACANTE, DA ;
DEANE, EF .
BIOLOGICALS, 1993, 21 (03) :275-286
[10]   ISOLATION OF PURE IGG1, IGG2A AND IGG2B IMMUNOGLOBULINS FROM MOUSE SERUM USING PROTEIN A-SEPHAROSE [J].
EY, PL ;
PROWSE, SJ ;
JENKIN, CR .
IMMUNOCHEMISTRY, 1978, 15 (07) :429-436