| Autor: | Makoto Takeuchi, Hirofumi Arai, Toshiko Kutsukake, Toshinori Watanabe, Hiroyuki Saitoh, Noboru Inoue, Haruhiko Tsumura |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
chemistry.chemical_classification
biology Chinese hamster ovary cell Recombinant Human Thrombopoietin Cell Biology Biochemistry Molecular biology law.invention Protein structure chemistry law Glycosyltransferase biology.protein Recombinant DNA Glycoside hydrolase Glycoprotein Molecular Biology Thrombopoietin |
| Zdroj: | Glycoconjugate Journal. 16:707-718 |
| ISSN: | 0282-0080 |
| DOI: | 10.1023/a:1007159409961 |
| Popis: | Human thrombopoietin (TPO) that regulates the numbers of megakaryocytes and platelets is a heavily N- and O-glycosylated glycoprotein hormone with partial homology to human erythropoietin (EPO). We prepared recombinant human TPO produced in Chinese hamster ovary (CHO) cells and analyzed the sugar chain structures quantitatively using 2-aminobenzamide labeling, sequential glycosidase digestion and matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF/MS). We found bi-, tri- and tetraantennary complex-type sugar chains with one or two N-acetyllactosamine repeats, which are common to recombinant human EPO produced in CHO cells. On the other hand, there were triantennary sugar chains with one or two N-acetyllactosamine repeats that were specific to the recombinant human TPO, and their distributions of branch structures were also different. These results suggested that proximal protein structure should determine the branch structure of Asn-linked sugar chains in addition to the glycosyltransferases subset. |
| Databáze: | OpenAIRE |
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