Abstract
This paper attempts to review the experimental efforts made to produce recombinant human erythropoietin. In view of its clinical importance, special attention must be paid to its quality in the sense of a functional replacement of the natural hormone. Accordingly, a detailed comparison of the human urinary extracted form with the recombinant product is given. For better understanding, the efforts at cloning and expression of the hormone in various cellular systems are discussed.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Lin F-K, Suggs S, Lin C-H et al. (1985) Cloning and expression of the human erythropoietin gene. Proc Natl Acad Sci USA 82, 7580–7584.
Lee-Huang S (1984) Cloning and expression of human erythropoietin cDNA in Escherichia coli. Proc Natl Acad Sci USA 81, 2708–2712.
Miyake T, Kung CK-H, Goldwasser E (1977) Purification of human erythropoietin. J Biol Chem 252, 5558–5564.
Lai PH, Everett R, Wang FF et al. (1986) Structural characterization of human erythropoietin. J Biol Chem 261, 3116–3121
Recny JM, Scoble HA, Kim Y (1987) Structural characterization of natural human urinary and recombinant DNA-derived erythropoietin. Identification of des-arginine 166 erythropoietin. J Biol Chem 262, 17156–17163.
Sytkowski MA, Fischer JW (1985) Isolation and characterization of an anti-peptide monoclonal antibody to human erythropoietin. J Biol Chem 260, 14727–14731.
Davis JM, Arakawa T, Strickland TW et al. (1987) Characterization of recombinant human erythropoietin produced in Chinese hamster ovary cells. Biochemistry 26, 2633–2638.
Sasaki H, Bothner B, Dell A et al. (1987) Carbohydrate structure of erythropoietin expressed in Chinese hamster ovary cells by a human erythropoietin cDNA. J Biol Chem 262, 12059–12076.
Takeuchi M, Takasaki S, Miyazaki H, et al. (1988) Comparative study of the asparagine linked sugar chains of human erythropoietins purified from urine and the culture medium of recombinant Chinese hamster ovary cells. J Biol Chem 263, 3657–3663.
Wojchowski DM, Orkin SH, Sytkowsky AJ (1987) Active human erythropoietin expressed in insect cells using a baculovirus vector: a role for N-linked oligosaccharide, Biochim Biophys Acta 910, 224–232.
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1989 Springer-Verlag Berlin Heidelberg
About this paper
Cite this paper
Battersby, R.V., Holloway, C.J. (1989). Recombinant Human Erythropoietin. In: Jelkmann, W., Gross, A.J. (eds) Erythropoietin. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-83745-6_12
Download citation
DOI: https://doi.org/10.1007/978-3-642-83745-6_12
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-83747-0
Online ISBN: 978-3-642-83745-6
eBook Packages: Springer Book Archive