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Expression of a differentiation antigen and poly-N-acetyllactosaminyl O-glycans directed by a cloned core 2 beta-1,6-N-acetylglucosaminyltransferase.
Chinese hamster ovary (CHO) cells do not contain detectable amounts of core 2 beta-1,6-N-acetylglucosaminyltransferase, C2GnT, and thus lack various modifications in their branched O-linkedExpand
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Poly-N-acetyllactosaminyl O-glycans attached to leukosialin. The presence of sialyl Le(x) structures in O-glycans.
Poly-N-acetyllactosamine extension has been found in O-glycans in addition to N-glycans and glycosphingolipids. Attempts were made in HL-60 and K562 cells to determine the amount ofExpand
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Genomic organization of core 2 and I branching beta-1,6-N-acetylglucosaminyltransferases. Implication for evolution of the beta-1,6-N-acetylglucosaminyltransferase gene family.
Two human beta-1,6-N-acetylglucosaminyltransferases forming the core 2 O-glycan branch, C2GnT and the I antigen, IGnT, are homologous to each other in three regions of the catalytic domain (A, B, C)Expand
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Sialyl Lex structures in O-glycans attached to lysosomal membrane glycoproteins, lamp-1 and lamp-2. Comparison to those in N-glycans.
Abstract Poly- N -acetyllactosamine extension has been found in O -glycans in addition to N -glycans and glycosphingolipids (Fukuda, M. (1994) In Molecular Glycobiology , (ed. M. Fukuda and O.Expand
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Isolation and characterization of a pseudogene related to human core 2 β-1,6-N-acetylglucosaminyltransferase
In a previous study, we isolated genomic clones encoding core 2β-1,6-N-acetylglucosaminyltransferase (C2GnT) and blood group IGnT and proposed that these two genes were produced from a commonExpand
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Isolation and characterization of a pseudogene related to human core 2 beta-1,6-N-acetylglucosaminyl-transferase.
In a previous study, we isolated genomic clones encoding core 2 beta-1,6-N-acetylglucosaminyltransferase (C2GnT) and blood group IGnT and proposed that these two genes were produced from a commonExpand