Separation of nonfucosylated antibodies with immobilized FcγRIII receptors. (1st April 2013)

• Record Type: Journal Article
• Authors: Bolton, Glen R.; Ackerman, Margaret E.; Boesch, Austin W.
• Is Part Of: Biotechnology progress. Volume 29:Number 3(2013:May/Jun.)
• Page Start: 825
• Page End: 828
• Publication Date: 2013-04-01
• Subjects: Biotechnology -- Periodicals; Food industry and trade -- Periodicals; Bioengineering -- Periodicals; 660.6
• DOI: 10.1002/btpr.1717
• Languages: English
• ISSNs: 8756-7938

Abstract

<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Post‐translational modifications can dramatically impact protein activity, but identifying such structure:function relationships, as well as capitalizing on functionally enhanced variants, is a significant challenge. Here, affinity chromatography resins that contained immobilized FcγRIII receptors were used to enrich nonfucosylated antibodies 6‐ to 9‐fold, offering what may be a tractable method for both the identification of post‐translational modifications that affect function, as well as a means to enrich variants with enhanced activity. © 2013 American Institute of Chemical Engineers <italic>Biotechnol. Prog</italic>., 29:825–828, 2013</p> </abstract>