Unambiguous Identification of Pyroglutamate in Full-Length Biopharmaceutical Monoclonal Antibodies by NMR Spectroscopy-Reference-Cited by-同舟云学术

Unambiguous Identification of Pyroglutamate in Full-Length Biopharmaceutical Monoclonal Antibodies by NMR Spectroscopy

Published:2019-10-07 Issue:22 Volume:91 Page:14299-14305
ISSN:0003-2700
Container-title:Analytical Chemistry
language:en
Short-container-title:Anal. Chem.

Author:

Hinterholzer Arthur¹²^ORCID,Stanojlovic Vesna²^ORCID,Cabrele Chiara¹²^ORCID,Schubert Mario¹²^ORCID

Affiliation:

1. Christian Doppler Laboratory for Innovative Tools for Biosimilar Characterization, University of Salzburg, Hellbrunnerstrasse 34, 5020 Salzburg, Austria

2. Department of Biosciences, University of Salzburg, Billrothstrasse 11, 5020 Salzburg, Austria

Funder

Bundesministerium f?r Wissenschaft, Forschung und Wirtschaft

State of Salzburg

Publisher

American Chemical Society (ACS)

Subject

Analytical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.analchem.9b02513

Reference36 articles.

1. Glutaminyl cyclases from animals and plants: a case of functionally convergent protein evolution

2. Characterization of Therapeutic Antibodies and Related Products

3. Protein amino-terminal modifications and proteomic approaches for N-terminal profiling

4. Formation of Pyroglutamic Acid from N-Terminal Glutamic Acid in Immunoglobulin Gamma Antibodies

5. Characterization of the stability of a fully human monoclonal IgG after prolonged incubation at elevated temperature

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