Rapid analytical tryptic mapping of a recombinant chimeric monoclonal antibody and method validation challenges

Kannan, K.; Mulkerrin, Michael G.; Zhang, M; Gray, Richard W.; Steinharter, T; Sewerin, K; Baffi, R; Harris, Reed J.; Karunatilake, Chandima

doi:10.1016/s0731-7085(97)00179-9

Cited by 21 publications

(7 citation statements)

References 5 publications

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“…One of the powerful tools of proteome study is obtaining peptide maps via protein digestion followed by MS identification and data processing. Initially, protein digestion was performed by in‐solution approach , which is time consuming, tedious, and inconvenient for automation. Nowadays, it is obvious that these drawbacks can be easily overcome by the application of immobilized enzymes.…”

Section: Application Of Flow‐through Monolithic Bioreactorsmentioning

confidence: 99%

Flow‐through immobilized enzyme reactors based on monoliths: II. Kinetics study and application

Влах

Tennikova

2013

J of Separation Science

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In the last decade, the application of monolithic materials has rapidly expanded to the realization of flow-through bioconversion processes. Up to these days, different classes of enzymes such as hydrolases, lyases, and oxidoreductases have been immobilized on organic, inorganic, or hybrid monolithic materials to prepare the effective flow-through enzymes reactors for application in proteomics, biotechnology, pharmaceutics, organic synthesis, and biosensoring. Current review describes the results of kinetic study and specialties of flow-through immobilized enzyme reactors based on the existing monolithic materials.

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Section: Application Of Flow‐through Monolithic Bioreactorsmentioning

confidence: 99%

Flow‐through immobilized enzyme reactors based on monoliths: II. Kinetics study and application

Влах

Tennikova

2013

J of Separation Science

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“…One common method to evaluate the primary structure (identity) of a monoclonal antibody and other protein-based pharmaceuticals such as FC fusion proteins and immunoconjugates is peptide mapping [2][3][4][5][6][7]. This method was often reserved for comparability but recently is moving into many modern stability programs and lot release tests making it necessary for a quick yet effective method [8]. Peptide mapping is also utilized in extended characterization of a drug candidate for complete analysis of primary sequence [9].…”

Section: Introductionmentioning

confidence: 99%

Peptide mapping of therapeutic monoclonal antibodies: Improvements for increased speed and fewer artifacts

Dick¹,

Mahon²,

Qiu³

et al. 2009

Journal of Chromatography B

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“…Analysis of the component peptides from enzymatic digestion of recombinant proteins can be used to locate PTMs, amino acid degradation products, glycosylation sites, and disulfide linkages within specific regions of the protein sequence. This approach is used commonly in biotechnology development as a fingerprint for identity testing, for process monitoring, and to demonstrate product comparability following manufacturing changes (Kannan et al, 1997;Schenerman et al, 1999;Bongers et al, 2000).…”

Section: Analysis Of Protein Digest Mixtures (''Bottom-up'' or Pepmentioning

confidence: 99%

“…For example, Figure 8 compares LC-UV chromatograms for tryptic digests of three different production lots of a monoclonal antibody to that of a reference standard (Kannan et al, 1997). Kannan et al showed that overall, the LC-UV chromatographic profiles look very similar with respect to peak shape and relative intensity, thus demonstrating that the products are comparable.…”

Section: Product Comparability Testingmentioning

confidence: 99%

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Applications of mass spectrometry for the structural characterization of recombinant protein pharmaceuticals

Barnes

Lim

2007

Mass Spectrometry Reviews

164

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Therapeutic proteins produced using recombinant DNA technologies are generally complex, heterogeneous, and subject to a variety of enzymatic or chemical modifications during expression, purification, and long-term storage. The use of mass spectrometry (MS) for the evaluation of recombinant protein sequence and structure provides detailed information regarding amino acid modifications and sequence alterations that have the potential to affect the safety and activity of therapeutic protein products. General MS approaches for the characterization of recombinant therapeutic protein products will be reviewed with particular attention given to the standard MS tools available in most biotechnology laboratories. A number of recent examples will be used to illustrate the utility of MS strategies for evaluation of recombinant protein heterogeneity resulting from post-translational modifications (PTMs), sequence variations generated from proteolysis or transcriptional/translational errors, and degradation products which are formed during processing or final product storage. Specific attention will be given to the MS characterization of monoclonal antibodies as a model system for large, glycosylated, recombinant proteins. Detailed examples highlighting the use of MS for the analysis of monoclonal antibody glycosylation, deamidation, and disulfide mapping will be used to illustrate the application of these techniques to a wide variety of heterogeneous therapeutic protein products. The potential use of MS to support the selection of cell line/clone selection and formulation development for therapeutic antibody products will also be discussed.

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Rapid analytical tryptic mapping of a recombinant chimeric monoclonal antibody and method validation challenges

Cited by 21 publications

References 5 publications

Flow‐through immobilized enzyme reactors based on monoliths: II. Kinetics study and application

Flow‐through immobilized enzyme reactors based on monoliths: II. Kinetics study and application

Peptide mapping of therapeutic monoclonal antibodies: Improvements for increased speed and fewer artifacts

Applications of mass spectrometry for the structural characterization of recombinant protein pharmaceuticals

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