Comparative Assessment of Glycosylation of a Recombinant Human FSH and a Highly Purified FSH Extracted from Human Urine

• DOI: 10.1021/acs.jproteome.5b00921
• Publication Date: 2016-01-26T18:33:54Z
• Authors: Hong Wang; Xi Chen; Xiaoxi Zhang; Wei Zhang; Yan Li; Hongrui Yin; Hong Shao; Gang Chen
• Keywords: N-linked glycosylation

Glycosylation is an important PTM and critical for the manufacture efficacy of therapeutic glycoproteins. Glycan significantly influences biological properties human follicle-stimulating hormone (hFSH). Using a glycoproteomic strategy, this study compared glycosylation putative highly purified FSH (uhFSH) obtained from urine with that recombinant (rhFSH) Chinese hamster ovary (CHO) cells. Intact subunit masses, N-glycans, N-glycosylation sites, intact N- O-glycopeptides were analyzed by mass spectrometry. Classic complementary analytical methods, including SDS-PAGE, isoelectric focusing, Steelman–Pohley bioassay also employed to compare their molecular weights, charge variants, specific activities. Results showed sialylated, branched, macro-heterogeneity glycans are predominant in uhFSH those rhFSH. The both hFSHs, which have not been described previously, characterized herein. A high degree heterogeneity was observed N-glycopeptides hFSHs. differences provide useful information elucidating further investigation glycan structures hFSH.