Publications
Detailed Information
In vitro galactosylation and sialylation of human immunoglobulin G : 인간유래 면역글로불린 G 단백질의 시험관내 갈락토실화 및 시알릴화 반응에 관한 연구
DC Field | Value | Language |
---|---|---|
dc.contributor.advisor | 김병기 | - |
dc.contributor.author | 정승욱 | - |
dc.date.accessioned | 2010-07-08T23:38:31Z | - |
dc.date.available | 2010-07-08T23:38:31Z | - |
dc.date.copyright | 2003. | - |
dc.date.issued | 2003 | - |
dc.identifier.uri | http://dcollection.snu.ac.kr:80/jsp/common/DcLoOrgPer.jsp?sItemId=000000057788 | - |
dc.identifier.uri | https://hdl.handle.net/10371/68546 | - |
dc.description | Thesis (master`s)--서울대학교 대학원 :응용화학부,2003. | en |
dc.description.abstract | Glycosylation is a common co- and post-translational modification of
proteins which may have profound effects on protein structure and function. Glycoproteins consist of an ensemble of glycosylated variants, or glycoforms, and the glycosylation pattern of a glycoprotein is not random but dependent on the cell type, physiological conditions, and in some carse disease states. For further studies to elucidate the structures and biological functions of the glycoproteins, the large amount of glycoproteins is needed, however it has been hard to produce recombinant glycoproteins with minimizing the heterogeneity as well as increasing the level of selective glycosylation. In this study, therefore, we have developed a versatile tool for in vitro synthesis of oligosaccharides and glycoconjugates using human immunoglobulin G as a model of therapeutic glycoprotein. Human IgG contains truncated glycans such as terminal galactose(Gal) and N-acetylglucosamine (GlcNAc) residues which may cause rapid clearance of IgG from circulation as a consequence of binding to the aglycosylprotein receptor. To increase the level of terminal sialylation, we regalactosylated and/or resialylated IgG using β1,4-galactosyltransferase and/or α 2,3-sialyltransferase by using UDP-Gal and CMP-NeuAc, respectively. And to overcome the difficulty associated with the preparation of sugar-nucleotides, efficient enzymatic systems for the production of UDP-Gal and CMP-NeuAc were introduced. | en |
dc.format.extent | 82 leaves | en |
dc.language.iso | en | en |
dc.publisher | 서울대학교 대학원 | en |
dc.subject | Glycoprotein | en |
dc.subject | N-linked oligosaccharides | en |
dc.subject | Immunoglobulin g | en |
dc.subject | Galactosyltransferase | en |
dc.subject | Sialyltransferase | en |
dc.subject | Udp-gal | en |
dc.subject | Cmp-neuac | en |
dc.title | In vitro galactosylation and sialylation of human immunoglobulin G | en |
dc.title.alternative | 인간유래 면역글로불린 G 단백질의 시험관내 갈락토실화 및 시알릴화 반응에 관한 연구 | en |
dc.type | Thesis | en |
dc.contributor.department | 응용화학부 | - |
dc.description.degree | Master | en |
- Appears in Collections:
- Files in This Item:
- There are no files associated with this item.
Item View & Download Count
Items in S-Space are protected by copyright, with all rights reserved, unless otherwise indicated.