Absence of Protein G-Fc Interaction in Ficin-Derived Mouse IgG sub(1) Digests

Typical procedure for IgG fragmentation is based on proteolytic cleavage at the hinge region and usually involves a post-digestion purification step. In mice, IgG sub(1) has been found to bind poorly to protein A. As a result, protein G chromatography could be considered as an alternative for Fc rem...

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Bibliographic Details
Published inJournal of immunoassay & immunochemistry Vol. 24; no. 3; pp. 311 - 318
Main Authors Belenky, A S, Wask-Rotter, E, Sommer, MJ
Format Journal Article
LanguageEnglish
Published 01.08.2003
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Summary:Typical procedure for IgG fragmentation is based on proteolytic cleavage at the hinge region and usually involves a post-digestion purification step. In mice, IgG sub(1) has been found to bind poorly to protein A. As a result, protein G chromatography could be considered as an alternative for Fc removal. Protein G is generally expected to bind specifically to the Fc region of IgG, but applying protein G for the purification of Fab sub(2) fragment of mouse monoclonal IgG sub(1) under standard physiological conditions, we obtained reproducible clone-independent negligible protein G-Fc reactivity and strong protein G-Fab sub(2) interaction.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
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ISSN:1532-1819
DOI:10.1081/IAS-120022940