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Article

Production of Highly Sialylated Recombinant Glycoproteins Using Ricinus communis Agglutinin-I-Resistant CHO Glycosylation Mutants.

Methods in molecular biology (Clifton, N.J.) - 1 Jan 2015

Goh John S Y, Chan Kah Fai, Song Zhiwei

Abstract excerpt

The degree of sialylation of therapeutic glycoproteins affects its circulatory half-life and efficacy because incompletely sialylated glycoproteins are cleared from circulation by asialoglycoprotein receptors present in the liver cells. Mammalian expression systems, often employed in the production of these glycoprotein drugs, produce heterogeneously sialylated products. Here, we describe how to produce highly...

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Source

Identifiers

PMID: 26082232
DOI: 10.1007/978-1-4939-2760-9_22

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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