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Data on Biotechnology Discussed by Researchers at University of Kansas (Characterization of Oxidative Carbonylation on Recombinant Monoclonal...

July 2, 2014



Data on Biotechnology Discussed by Researchers at University of Kansas (Characterization of Oxidative Carbonylation on Recombinant Monoclonal Antibodies)

By a News Reporter-Staff News Editor at Biotech Week -- Research findings on Biotechnology are discussed in a new report. According to news originating from Lawrence, Kansas, by NewsRx correspondents, research stated, "In the biotechnology industry, oxidative carbonylation as a post-translational modification of protein pharmaceuticals has not been studied in detail. Using Quality by Design (gbD) principles, understanding the impact of oxidative carbonylation on product quality of protein pharmaceuticals, particularly from a site-specific perspective, is critical."

Our news journalists obtained a quote from the research from the University of Kansas, "However, comprehensive identification of carbonylation sites has so far remained a very difficult analytical challenge for the industry. In this paper, we report for the first time the identification of specific carbonylation sites on recombinant monoclonal antibodies with a new analytical approach via derivatization with Girard's Reagent T (GRT) and subsequent peptide mapping with high-resolution mass spectrometry. Enhanced ionization efficiency and high quality MS2 data resulted from GRT derivatization were observed as key benefits of this approach, which enabled direct identification of carbonylation sites without any fractionation or affinity enrichment steps. A simple data filtering process was also incorporated to significantly reduce false positive assignments. Sensitivity and efficiency of this approach were demonstrated by identification of carbonylation sites on both unstressed and oxidized antibody bulk drug substances. The applicability of this approach was further demonstrated by identification of 14 common carbonylation sites on three highly similar IgG1s."

According to the news editors, the research concluded: "Our approach represents a significant improvement to the existing analytical methodologies and facilitates extended characterization of oxidative carbonylation on recombinant monoclonal antibodies and potentially other protein pharmaceuticals in the biotechnology industry."

For more information on this research see: Characterization of Oxidative Carbonylation on Recombinant Monoclonal Antibodies. Analytical Chemistry, 2014;86(10):4799-4806. Analytical Chemistry can be contacted at: Amer Chemical Soc, 1155 16TH St, NW, Washington, DC 20036, USA. (American Chemical Society - www.acs.org; Analytical Chemistry - www.pubs.acs.org/journal/ancham)

The news correspondents report that additional information may be obtained from Y. Yang, University of Kansas, Dept. of Pharmaceut Chem, Lawrence, KS 66047, United States. Additional authors for this research include C. Stella, W.R. Wang, C. Schoneich and L. Gennaro (see also Biotechnology).

Keywords for this news article include: Biotechnology, Kansas, Lawrence, Immunology, United States, Blood Proteins, Immunoglobulins, Serum Globulins, Monoclonal Antibodies, North and Central America

Our reports deliver fact-based news of research and discoveries from around the world. Copyright 2014, NewsRx LLC


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Source: Biotech Week


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