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Sci. Pharm. 2015, 83(2), 401-410; doi:10.3797/scipharm.1501-12

Suppression of IgM Proteolysis by Conformational Stabilization Through Excipients

1
Department of Pharmaceutical Technology and Biopharmaceutics, University of Vienna, Althanstrasse 14, A-1090 Vienna, Austria.
2
Bioprocessing Technology Institute, A*STAR, 20 Biopolis Way, #06-01, Centros, 138668, Singapore.
*
Author to whom correspondence should be addressed.
Received: 21 January 2015 / Accepted: 4 March 2015 / Published: 4 March 2015
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Abstract

Protease activity from host cell lines may cause product loss or affect the quality of recombinant proteins. In this study, we showed that excipients like glycine and sorbitol reduce the proteolysis of an immunoglobulin M (IgM) in the presence of added proteases like α-chymotrypsin, papain, and pepsin. The activity of the proteases in the IgM-protective environments was conserved or even enhanced as tested using low molecular weight substrates. Thus, a higher resistance against proteolytic degradation appears to be caused by the conformational stabilization of the IgM due to preferential exclusion of sorbitol and glycine.
Keywords: IgM; Proteolysis; Conformational stability; Sorbitol; Glycine IgM; Proteolysis; Conformational stability; Sorbitol; Glycine
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

MUELLER, M.; LOH, M.Q.T.; GAGNON, P. Suppression of IgM Proteolysis by Conformational Stabilization Through Excipients. Sci. Pharm. 2015, 83, 401-410.

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