Author: ["Masaaki Goto","Kunihisa Akai","Akihiko Murakami","Chika Hashimoto","Eisuke Tsuda","Masatsugu Ueda","Gosei Kawanishi","Noriko Takahashi","Akimine Ishimoto","Hideo Chiba","Ryuzo Sasaki"]
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Abstract
Erythropoietin (EPO), a heavily glycosylated protein, is a major stimulatory factor in erythropoiesis. The human EPO gene was engineered for expression in animal cells. Recombinant EPOs produced in two kinds of cells were isolated and their properties compared with those of human urinary EPO. The results indicated that the carbohydrates attached to the EPO peptide are responsible for the different biological activities of these proteins. The biological activities of recombinant glycoproteins produced in heterologous systems may vary depending on the host cells in which the proteins are modified.Cite this article
Goto, M., Akai, K., Murakami, A. et al. Production of Recombinant Human Erythropoietin in Mammalian Cells: Host–Cell Dependency of the Biological Activity of the Cloned Glycoprotein. Nat Biotechnol 6, 67–71 (1988). https://doi.org/10.1038/nbt0188-67 