Emerging methods for the production of homogeneous human glycoproteins
Most circulating human proteins exist as heterogeneously glycosylated variants (glycoforms) of an otherwise homogeneous polypeptide. Though glycan heterogeneity is most likely important to glycoprotein function, the preparation of homogeneous glycoforms is important both for the study of the consequ...
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Published in | Nature chemical biology Vol. 5; no. 4; pp. 206 - 215 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
New York
Nature Publishing Group US
01.04.2009
Nature Publishing Group |
Subjects | |
Online Access | Get full text |
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Summary: | Most circulating human proteins exist as heterogeneously glycosylated variants (glycoforms) of an otherwise homogeneous polypeptide. Though glycan heterogeneity is most likely important to glycoprotein function, the preparation of homogeneous glycoforms is important both for the study of the consequences of glycosylation and for therapeutic purposes. This review details selected approaches to the production of homogeneous human N- and O-linked glycoproteins with human-type glycans. Particular emphasis is placed on recent developments in the engineering of glycosylation pathways within yeast and bacteria for
in vivo
production, and on the
in vitro
remodeling of glycoproteins by enzymatic means. The future of this field is very exciting. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 ObjectType-Article-2 ObjectType-Feature-3 ObjectType-Review-1 |
ISSN: | 1552-4450 1552-4469 |
DOI: | 10.1038/nchembio.148 |