Method to convert N-terminal glutamine to pyroglutamate for characterization of recombinant monoclonal antibodies
| Autor: | Yan Peng, Daisy Richardson, Wei Xu, Fengqiang Wang, Brittany C. Paporello, Hongcheng Liu |
|---|---|
| Rok vydání: | 2012 |
| Předmět: |
medicine.drug_class
Glutamine Biophysics Monoclonal antibody Biochemistry Mass Spectrometry law.invention Liquid chromatography–mass spectrometry law medicine Molecular Biology Chromatography High Pressure Liquid chemistry.chemical_classification Chromatography biology Antibodies Monoclonal Cell Biology Glutaminyl-Peptide Cyclotransferase Recombinant Proteins Amino acid Pyrrolidonecarboxylic Acid Enzyme chemistry Cyclization biology.protein Recombinant DNA Biocatalysis Antibody |
| Zdroj: | Analytical biochemistry. 436(1) |
| ISSN: | 1096-0309 |
| Popis: | Cyclization of N-terminal glutamine to pyroglutamate is a common modification of recombinant monoclonal antibodies that has often been identified by liquid chromatography mass spectrometry (LC-MS) analysis using separated fractions. An alternative approach of using glutaminyl-peptide cyclotransferase to convert the N-terminal glutamine to pyroglutamate was developed in the current study. Enzymatic conversion of the N-terminal glutamine to pyroglutamate not only provides an identification of the N-terminal amino acids without fraction collection but also can significantly simplify the chromatograms to assist fraction collections for the characterization of other antibody variants. |
| Databáze: | OpenAIRE |
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