Abstract:
:The transfection of glycoprotein glycosyltransferase genes into cells leads to modification of both the structure and function of the glycoproteins and as a result, changes in glycome patterns. N-glycan branching enzymes hold some promise as a model system for the identification of glycome patterns. Both N-acetylglucosaminyltransferase III and alpha 1-6 fucosyltransferase are typical glycosyltransferases, which are involved in the branching of N-glycans. The resulting enzymatic products, bisecting N-GlcNAc and alpha 1-6 fucose residues, are no longer modified by other glycosyltransferases and it is a relatively simple task to identify their modification by means of lectins. In this review, the glycome patterns of glycosyltransferase gene transfectants and the non-transfectants were compared by two-dimensional gel electrophoresis and lectin staining, and the biological significance of the two genes are described. Analyses of glycome patterns by transfecting glycosyltransferase genes will lead to new fields of study in the area of postgenome research.
journal_name
Proteomicsjournal_title
Proteomicsauthors
Taniguchi N,Ekuni A,Ko JH,Miyoshi E,Ikeda Y,Ihara Y,Nishikawa A,Honke K,Takahashi Mdoi
10.1002/1615-9861(200102)1:2<239::AID-PROT239>3.0.subject
Has Abstractpub_date
2001-02-01 00:00:00pages
239-47issue
2eissn
1615-9853issn
1615-9861journal_volume
1pub_type
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