Unusual N-glycosylation of a recombinant human erythropoietin expressed in a human lymphoblastoid cell line does not alter its biological properties
Author:
Publisher
Oxford University Press (OUP)
Subject
Biochemistry
Link
http://academic.oup.com/glycob/article-pdf/10/5/511/9806133/100511.pdf
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3. Characterization of the structural determinants required for the high affinity interaction of asparagine-linked oligosaccharides with immobilized Phaseolus vulgaris leukoagglutinating and erythroagglutinating lectins.
4. Role of glycosylation on the secretion and biological activity of erythropoietin
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1. Effect of Cell Culture Process Parameters on Glycosylation and in Vivo Biological Activity of Recombinant Human Erythropoietin;2024
2. Glycoengineering tobacco plants to stably express recombinant human erythropoietin with different N-glycan profiles;International Journal of Biological Macromolecules;2020-08
3. Multi-Attribute Monitoring of Complex Erythropoetin Beta Glycosylation by GluC Liquid Chromatography–Mass Spectrometry Peptide Mapping;Analytical Chemistry;2020-05-19
4. Comprehensive Characterization ofN‐Glycosylation in Darbepoetin Alfa;Bulletin of the Korean Chemical Society;2019-08-30
5. Structure-Function Relationships for Recombinant Erythropoietins: A Case Study From a Proposed Manufacturing Change With Implications for Erythropoietin Biosimilar Study Designs;Journal of Pharmaceutical Sciences;2018-06
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