Academic Journal

Immunoglobulin G elution in protein A chromatography employing the method of chromatofocusing for reducing the co‐elution of impurities

التفاصيل البيبلوغرافية
العنوان: Immunoglobulin G elution in protein A chromatography employing the method of chromatofocusing for reducing the co‐elution of impurities
المؤلفون: Pinto, Nuno D.S., Uplekar, Shaunak D., Moreira, Antonio R., Rao, Govind, Frey, Douglas D.
المساهمون: National Science Foundation
المصدر: Biotechnology and Bioengineering ; volume 114, issue 1, page 154-162 ; ISSN 0006-3592 1097-0290
بيانات النشر: Wiley
سنة النشر: 2016
المجموعة: Wiley Online Library (Open Access Articles via Crossref)
الوصف: Purification processes for monoclonal Immunoglobulin G (IgG) typically employ protein A chromatography as a capture step to remove most of the impurities. One major concern of the post‐protein A chromatography processes is the co‐elution of some of the host cell proteins (HCPs) with IgG in the capture step. In this work, a novel method for IgG elution in protein A chromatography that reduces the co‐elution of HCPs is presented where a two‐step pH gradient is self‐formed inside a protein A chromatography column. The complexities involved in using an internally produced pH gradient in a protein A chromatography column employing adsorbed buffering species are discussed though equation‐based modeling. Under the conditions employed, ELISA assays show a 60% reduction in the HCPs co‐eluting with the IgG fraction when using the method as compared to conventional protein A elution without affecting the IgG yield. Evidence is also obtained which indicates that the amount of leached protein A present in free solution in the purified product is reduced by the new method. Biotechnol. Bioeng. 2017;114: 154–162. © 2016 Wiley Periodicals, Inc.
نوع الوثيقة: article in journal/newspaper
اللغة: English
DOI: 10.1002/bit.26053
الاتاحة: http://dx.doi.org/10.1002/bit.26053
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رقم الانضمام: edsbas.CCDC25E2
قاعدة البيانات: BASE