Uniform [13C,15N]-labeled and glycosylated IgG1 Fc expressed in Saccharomyces cerevisiae

Despite the prevalence and importance of glycoproteins in human biology, methods for isotope labeling suffer significant limitations. Common prokaryotic platforms do not produce mammalian post-translation modifications that are essential to the function of many human glycoproteins, including immunog...

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Veröffentlicht in:	Journal of biomolecular NMR 2024-03, Vol.78 (1), p.9-18
Hauptverfasser:	Davis, Alexander R., Roberts, Elijah T., Amster, I. Jonathan, Barb, Adam W.
Format:	Artikel
Sprache:	eng
Schlagworte:	Ammonium Ammonium chloride Animals Biochemistry Biological and Medical Physics Biophysics Complex media Complexity Culture E coli Escherichia coli Fungi Glycoproteins Glycoproteins - chemistry Humans Immunoglobulin Fc Fragments - chemistry Immunoglobulin G Immunoglobulin G - chemistry Labeling Mammals Mass spectrometry Mass spectroscopy Nitrogen isotopes NMR Nuclear magnetic resonance Nuclear Magnetic Resonance, Biomolecular - methods Physics Physics and Astronomy Polypeptides Post-translation Saccharomyces cerevisiae Spectroscopy/Spectrometry Yeast
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