The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.
Comparative study of the asparagine-linked sugar chains of human erythropoietins purified from urine and the culture medium of recombinant Chinese hamster ovary cells.
Open accessAbstract
The asparagine-linked sugar chains of human erythropoietin produced by recombinant Chinese hamster ovary cells and naturally occurring human urinary erythropoietin were liberated by hydrazinolysis and fractionated by paper electrophoresis, lectin affinity chromatography, and Bio-Gel P-4 column chromatography. Both erythropoietins had three asparagine-linked sugar chains in one molecule, all of which were acidic complex type. Structural analysis of them revealed that the sugar chains from both erythropoietins are quite similar except for sialyl linkage. All sugar chains of erythropoietin produced by recombinant Chinese hamster ovary cells contain only the NeuAc alpha 2----3Gal linkage, while those of human urinary erythropoietin contain the NeuAc alpha 2----6Gal linkage together with the NeuAc alpha 2----3Gal linkage. The major sugar chains were of fucosylated tetraantennary complex type with and without N-acetyllactosamine repeating units in their outer chain moieties in common, and small amounts of 2,4- and 2,6-branched triantennary and biantennary sugar chains were detected. This paper proved, for the first time, that recombinant technique can produce glycoprotein hormone whose carbohydrate structures are common to the major sugar chains of the native one.
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Isolation and characterization of genomic and cDNA clones of human erythropoietin
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Self-citationFractionation of Glycopeptides by Affinity Column Chromatography on Concanavalin A-Sepharose1
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Self-citation[90] α-Mannosidase, β-N-acetylhexosaminidase, and β-galactosidase from jack bean meal
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Self-citationCharacterization of recombinant human erythropoietin produced in Chinese hamster ovary cells
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Cited by
Varki, A. (2017) · Glycobiology · doi:10.1093/glycob/cww086 · Cited by 2,635
“The size, number, branching and degree of sialylation of N-glycans can generate numerous glycoforms of a single polypeptide such as erythropoietin (629) (630) (631) (632) (633) (634) (635) (636) (637) (638) (639) (640) or GM-CSF (641) (642) (643) (644) .”
BackgroundPaulson, J. C., & Colley, K. J. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84610-0 · Cited by 909
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Metadata
- Authors
- Takeuchi, M., Takasaki, S., Miyazaki, H., Kato, T., Hoshi, S., Kochibe, N., & Kobata, A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1988-03
- Volume
- 263
- Issue
- 8
- Pages
- 3657-3663
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1570484367
- Cited by
- 307
- References
- 30
- FWCI
- 7.62
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Takeuchi, M., Takasaki, S., Miyazaki, H., Kato, T., Hoshi, S., Kochibe, N., & Kobata, A. (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. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)68975-6
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