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Article

Highly sialylated recombinant human erythropoietin production in large-scale perfusion bioreactor utilizing CHO-gmt4 (JW152) with restored GnT I function.

Biotechnology journal - 1 Jan 2014

Goh John S Y, Liu Yingwei, Liu Haifeng, Chan Kah Fai, Wan Corrine, Teo Gavin, Zhou Xiangshan, Xie Fusheng, Zhang Peiqing, Zhang Yuanxing, Song Zhiwei

Abstract excerpt

Therapeutic glycoprotein drugs require a high degree of sialylation of their N-glycans for a better circulatory half-life that results in greater efficacy. It has been demonstrated that Chinese hamster ovary (CHO) glycosylation mutants lacking N-acetylglucosaminyltransferase I (GnT I), when restored by introduction of a functional GnT I, produced highly sialylated erythropoietin (EPO). We have now further...

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Identifiers

PMID: 24166780
DOI: 10.1002/biot.201300301

Genes

EPO
DHFR

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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