| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-150 |
Sentence |
denotes |
Molecular cloning and enzymatic characterization of a UDP-GalNAc:GlcNAc(beta)-R beta1,4-N-acetylgalactosaminyltransferase from Caenorhabditis elegans. |
| T2 |
151-294 |
Sentence |
denotes |
A common terminal structure in glycans from animal glycoproteins and glycolipids is the lactosamine sequence Gal(beta)4GlcNAc-R (LacNAc or LN). |
| T3 |
295-431 |
Sentence |
denotes |
An alternative sequence that occurs in vertebrate as well as in invertebrate glycoconjugates is GalNAc(beta)4GlcNAc-R (LacdiNAc or LDN). |
| T4 |
432-589 |
Sentence |
denotes |
Whereas genes encoding beta4GalTs responsible for LN synthesis have been reported, the beta4GalNAcT(s) responsible for LDN synthesis has not been identified. |
| T5 |
590-795 |
Sentence |
denotes |
Here we report the identification of a gene from Caenorhabditis elegans encoding a UDP-GalNAc:GlcNAc(beta)-R beta1,4-N-acetylgalactosaminyltransferase (Ce(beta)4GalNAcT) that synthesizes the LDN structure. |
| T6 |
796-932 |
Sentence |
denotes |
Ce(beta)4GalNAcT is a member of the beta4GalT family, and its cDNA is predicted to encode a 383-amino acid type 2 membrane glycoprotein. |
| T7 |
933-1200 |
Sentence |
denotes |
A soluble, epitope-tagged recombinant form of Ce(beta)4GalNAcT expressed in CHO-Lec8 cells was active using UDP-GalNAc, but not UDP-Gal, as a donor toward a variety of acceptor substrates containing terminal beta-linked GlcNAc in both N- and O-glycan type structures. |
| T8 |
1201-1319 |
Sentence |
denotes |
The LDN structure of the product was verified by co-chromatography with authentic standards and (1)H NMR spectroscopy. |
| T9 |
1320-1560 |
Sentence |
denotes |
Moreover, Chinese hamster ovary CHO-Lec8 and CHO-Lec2 cells expressing Ce(beta)4GalNAcT acquired LDN determinants on endogenous glycoprotein N-glycans, demonstrating that the enzyme is active in mammalian cells as an authentic beta4GalNAcT. |
| T10 |
1561-1715 |
Sentence |
denotes |
The identification and availability of this novel enzyme should enhance our understanding of the structure and function of LDN-containing glycoconjugates. |
