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Suppression of IgM Proteolysis by Conformational Stabilization Through Excipients
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 peps...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Austrian Journal of Pharmaceutical Sciences
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4727821/ https://www.ncbi.nlm.nih.gov/pubmed/26839826 http://dx.doi.org/10.3797/scipharm.1501-12 |
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author | Mueller, Monika Loh, Maybelle Q. T. Gagnon, Pete |
author_facet | Mueller, Monika Loh, Maybelle Q. T. Gagnon, Pete |
author_sort | Mueller, Monika |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-4727821 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | The Austrian Journal of Pharmaceutical Sciences |
record_format | MEDLINE/PubMed |
spelling | pubmed-47278212016-02-02 Suppression of IgM Proteolysis by Conformational Stabilization Through Excipients Mueller, Monika Loh, Maybelle Q. T. Gagnon, Pete Sci Pharm Research Article 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. The Austrian Journal of Pharmaceutical Sciences 2015 2015-03-04 /pmc/articles/PMC4727821/ /pubmed/26839826 http://dx.doi.org/10.3797/scipharm.1501-12 Text en Copyright: © Mueller et al. http://creativecommons.org/licenses/by/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Mueller, Monika Loh, Maybelle Q. T. Gagnon, Pete Suppression of IgM Proteolysis by Conformational Stabilization Through Excipients |
title | Suppression of IgM Proteolysis by Conformational Stabilization Through Excipients |
title_full | Suppression of IgM Proteolysis by Conformational Stabilization Through Excipients |
title_fullStr | Suppression of IgM Proteolysis by Conformational Stabilization Through Excipients |
title_full_unstemmed | Suppression of IgM Proteolysis by Conformational Stabilization Through Excipients |
title_short | Suppression of IgM Proteolysis by Conformational Stabilization Through Excipients |
title_sort | suppression of igm proteolysis by conformational stabilization through excipients |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4727821/ https://www.ncbi.nlm.nih.gov/pubmed/26839826 http://dx.doi.org/10.3797/scipharm.1501-12 |
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