EXAMPLES

Mass determination of native or recombinant protein or glycoprotein, synthetic peptide, nuclear receptor…

Peptide mapping of recombinant proteins and comparison between production batches 

Protein sequencing by LC/ESI-MS/MS and/or MALDI-PSD of recombinant proteins (18kD recombinant protein produced in E.coli, heavy and light chain of a recombinant IgG from mammalian cells)

Protein identification from 1D and 2D SDS-PAGE

Identification of HCP in production batches of a recombinant vaccine or a recombinant interleukin

Disulfide bridge characterization on interleukin or recombinant vaccines

Phosphorylation analysis on recombinant protein by MALDI-TOF and ESI-LC-MS/MS

N-terminal sequencing (Edman) of protein transferred to PVDF membrane

Amino Acid analysis to determine the protein concentration

Recombinant protein purification from plant (tobacco or corn), milk, secreted protein in supernatant of fermentation

Development of analytical methods for the quantification of metabolites in plasma samples

Determination of impurities and iso-forms in pharmaceutical formulations of synthetic peptides

Specific examples for glycosylation studies:

Glycoprofiling (analysis of the global N-glycan population) of different pharmaceutical glycoproteins (IgG, IgM, Interleukin, Coagulation Factors) from different production systems;

Determination of N- and O-glycosylation site occupation and identification of site specific glycan populations (IgG, IgM, Interleukin, other recombinant proteins);

Determination of sialic acid linkage (peptide hormone);

Confirmation of glycan structures by MS/MS or MALDI PSD (presence of Gal-α-Gal or of NAGA; IgM, IgG, Coagulation Factor);

O-glycosylation studies (Interleukin, coagulation factors);

Batch to batch comparison of glycosylation profiles for product development and quality control (IgM, IgG from CHO, NS0, Interleukin);

Quality control of recombinant glycoprotein batches by ESI-IT MS according to European Pharmacopeia

Glycoprofiling of target proteins for projects modifying the glycosylation machinery of host cells (bacteria, yeast, plants, transgenic animals)

Determination of the glycosylation potential of complex systems (bacteria, yeast, plants, eukaryotic non mammalian cell lines, transgenic animals)

Proteodynamics : Biopôle Clermont-Limagne - 63360 Saint Beauzire
Laboratory address : Proteodynamics / ZATE UMR 484 / BP184 rue Montalembert - 63005 Clermont-Ferrand cedex - France
Une création de l'agence web overscan