Characterization of Protein Glycoforms at Intact Level by Orbitrap Mass Spectrometry

Autor: Dan Bach, Kristensen, Trine Meiborg, Sloth, Martin, Ørgaard, Pernille Foged, Jensen

Publikováno v: Methods in molecular biology (Clifton, N.J.). 2271

Intact mass analysis of proteins is simple, fast, and specific, and it effectively provides structural insight into the proteoforms or variants of the analyzed protein. For instance, the multiple glycoforms of recombinant monoclonal antibodies can be

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ec89b11ad02f9c3ae3296f24b8dd6a34
https://pubmed.ncbi.nlm.nih.gov/33907997

Deglycosylation by the Acidic Glycosidase PNGase H+ Enables Analysis of N-Linked Glycoproteins by Hydrogen/Deuterium Exchange Mass Spectrometry

Autor: Pernille Foged Jensen, Ya Min Du, Kasper D. Rand, Jeppe B. Madsen, Josef Voglmeir, Gerard Comamala, Eva Christina Østerlund, Morten Beck Trelle, Thomas J. D. Jørgensen

Publikováno v: Comamala, G, Madsen, J B, Voglmeir, J, Du, Y M, Jensen, P F, Østerlund, E C, Trelle, M B, Jørgensen, T J D & Rand, K D 2020, ' Deglycosylation by the Acidic Glycosidase PNGase H + Enables Analysis of N-Linked Glycoproteins by Hydrogen/Deuterium Exchange Mass Spectrometry ', Journal of The American Society for Mass Spectrometry, vol. 31, no. 11, pp. 2305-2312 . https://doi.org/10.1021/jasms.0c00258

Hydrogen/deuterium exchange monitored by mass spectrometry (HDX-MS) has become an important method to study the structural dynamics of proteins. However, glycoproteins represent a challenge to the traditional HDX-MS workflow for determining the deute

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8763ef187ccc9951537240f268ccfd74
https://findresearcher.sdu.dk:8443/ws/files/183648430/Deglycosylation_by_the_acidic_glycosidase_PNGase_.pdf

A Two-pronged Binding Mechanism of IgG to the Neonatal Fc Receptor Controls Complex Stability and IgG Serum Half-life*

Autor: Maximiliane Hilger, Tilman Schlothauer, Vincent Larraillet, Angela Schoch, Kasper D. Rand, Thomas Emrich, Pernille Foged Jensen

Publikováno v: Jensen, P F, Schoch, A, Larraillet, V, Hilger, M, Schlothauer, T, Emrich, T & Rand, K D 2017, ' A Two-pronged Binding Mechanism of IgG to the Neonatal Fc Receptor Controls Complex Stability and IgG Serum Half-life ', Molecular and Cellular Proteomics, vol. 16, no. 3, pp. 451-456 . https://doi.org/10.1074/mcp.M116.064675

The success of recombinant monoclonal immunoglobulins (IgG) is rooted in their ability to target distinct antigens with high affinity combined with an extraordinarily long serum half-life, typically around 3 weeks. The pharmacokinetics of IgGs is int

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2461d4a9bf407633acc6ea607b6c85ce
https://europepmc.org/articles/PMC5341005/

Hydrogen Exchange

Autor: Pernille Foged Jensen, Kasper D. Rand

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::a7c9c30d35703cb016bb87030bb77534
https://doi.org/10.1002/9781118703748.ch1

Conformational Destabilization of Immunoglobulin G Increases the Low pH Binding Affinity with the Neonatal Fc Receptor*

Autor: Thomas W. Patapoff, Jennifer Y. Zhang, Benjamin T. Walters, Tilman Schlothauer, Kasper D. Rand, Vincent Larraillet, Pernille Foged Jensen, Kevin Lin

Crystallographic evidence suggests that the pH-dependent affinity of IgG molecules for the neonatal Fc receptor (FcRn) receptor primarily arises from salt bridges involving IgG histidine residues, resulting in moderate affinity at mildly acidic condi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed4c0b215cb3cce5ac550ccb7654a230
https://europepmc.org/articles/PMC4722460/