| Literature DB >> 20045465 |
Ka Fai Suen1, Mary S Turner, Feng Gao, Bo Liu, Alana Althage, Anthony Slavin, Weijia Ou, Elizabeth Zuo, Michael Eckart, Tomohisa Ogawa, Masao Yamada, Tove Tuntland, Jennifer L Harris, John W Trauger.
Abstract
Transient transfection of mammalian cells in suspension culture has recently emerged as a very useful method for production of research-scale quantities of recombinant proteins. The most commonly used cell lines for this purpose are suspension-adapted HEK and CHO cells. We report here that the plasma exposure in mice of an IL-23R extracellular domain Fc fusion protein (IL23R-Fc) differed dramatically depending on whether the protein was prepared by transient transfection of HEK or CHO cells. Specifically, IL23R-Fc expressed using CHO cells had about 30-fold higher in vivo plasma exposure compared to the HEK-expressed protein. In contrast to their differing plasma exposures, the HEK- and CHO-expressed proteins had equivalent in vitro biological activity. Characterization of the CHO- and HEK-expressed IL23R-Fc proteins indicated that the differences in in vivo plasma exposure between them are due to differential glycosylation. Copyright (c) 2010 Elsevier Inc. All rights reserved.Entities:
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Year: 2010 PMID： 20045465 DOI： 10.1016/j.pep.2009.12.015
Source DB: PubMed Journal: Protein Expr Purif ISSN： 1046-5928 Impact factor: 1.650