GO:0047223 beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0047223 describes an enzyme activity that adds N-acetylglucosamine (GlcNAc) in a beta-1,3 linkage to a galactose residue on O-glycosyl-glycoprotein substrates, using UDP-GlcNAc as the donor.
• This activity is a key elongation step in mucin-type O-glycan biosynthesis, extending core 1-derived structures to form core 2 and core 3 branches.
• The enzyme was biochemically characterized from swine trachea epithelium, where it acts on Gal beta 3(GlcNAc beta 6)GalNAc-mucin acceptors.
• Defects in related N-acetylglucosaminyltransferase activities cause carbohydrate-deficient glycoprotein syndrome type II, highlighting the clinical importance of this enzyme class.
• Research on glycosyltransferases often uses heterologous expression systems such as silkworm baculovirus or bacterial systems to produce active enzymes for functional and structural studies.
• Studying GO:0047223 helps clarify how altered O-glycosylation contributes to inflammatory and autoimmune conditions, as shown by N-glycan processing deficiencies in ocular autoimmune disease models.
Description
GO:0047223, beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity, is a molecular function that catalyzes the transfer of N-acetyl-D-glucosamine (GlcNAc) from UDP-GlcNAc to a beta-D-galactosyl-1,3-(N-acetyl-D-glucosaminyl-1,6)-N-acetyl-D-galactosaminyl-R acceptor, forming a beta-1,3 linkage on O-glycosyl-glycoprotein substrates. This reaction is a critical elongation step in the biosynthesis of mucin-type O-glycans, which are abundant on secreted and membrane-bound glycoproteins. The enzyme was first biochemically resolved from swine trachea epithelium, where it acts on core 2-based acceptors to extend the O-glycan chain. Because O-glycans influence protein stability, cell adhesion, and immune recognition, understanding this activity is essential for glycobiology and disease research. The enzyme belongs to the glycosyltransferase family and is distinct from beta-1,2-N-acetylglucosaminyltransferase II (MGAT2), which acts on N-glycans. While MGAT2 deficiency causes carbohydrate-deficient glycoprotein syndrome type II (CDG-II), a severe congenital disorder of glycosylation, the O-glycan-specific beta-1,3-N-acetylglucosaminyltransferase activity described by GO:0047223 has been less directly linked to a defined human disease, but it is part of the broader machinery that determines glycan structures relevant to inflammation and autoimmunity. Researchers study GO:0047223 to map O-glycan biosynthetic pathways, to produce recombinant enzymes for structural and kinetic analyses, and to understand how glycosylation defects contribute to disease. The activity is typically assayed using synthetic acceptors or mucin-derived substrates and requires divalent cations and UDP-GlcNAc as the donor. Advances in heterologous expression, including silkworm and bacterial systems, have enabled the production of active glycosyltransferases for detailed characterization.
beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity At A Glance
| GO ID | GO:0047223 |
|---|---|
| GO term | beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity |
| Ontology | molecular_function |
| Synonym | elongation 3-beta-GalNAc-transferase activity; O-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II activity; uridine diphosphoacetylglucosamine-mucin beta(1->3)-acetylglucosaminyltransferase (elongating) |
| Major function | Transfer of GlcNAc from UDP-GlcNAc to a beta-galactose residue on O-glycosyl-glycoprotein acceptors, forming a beta-1,3 linkage |
| Substrate | beta-D-galactosyl-1,3-(N-acetyl-D-glucosaminyl-1,6)-N-acetyl-D-galactosaminyl-R (core 2 or core 3 type O-glycan acceptor) |
| Donor | UDP-N-acetyl-D-glucosamine (UDP-GlcNAc) |
| Product | N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,6)-N-acetyl-D-galactosaminyl-R + UDP |
| Source organism (characterized) | Sus scrofa (swine trachea epithelium) |
What Is GO:0047223?
GO:0047223 is defined as the catalysis of the reaction: beta-D-galactosyl-1,3-(N-acetyl-D-glucosaminyl-1,6)-N-acetyl-D-galactosaminyl-R + UDP-N-acetyl-D-glucosamine = N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,6)-N-acetyl-D-galactosaminyl-R + UDP. In simpler terms, it is an enzyme activity that adds a GlcNAc sugar in a beta-1,3 linkage to a galactose residue on an O-glycosyl-glycoprotein acceptor, using UDP-GlcNAc as the sugar donor. This activity is also known as elongation 3-beta-GalNAc-transferase, O-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II, and uridine diphosphoacetylglucosamine-mucin beta(1->3)-acetylglucosaminyltransferase (elongating).
Why Is beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity Important in Cell Biology?
GO:0047223 is important because it defines a specific elongation step in O-glycan biosynthesis that shapes the structure and function of mucin-type glycoproteins. O-glycans are critical for protein stability, cell-cell recognition, and immune modulation, and their dysregulation is associated with inflammatory and autoimmune conditions. Although the enzyme activity itself has not been directly linked to a monogenic disease, related N-acetylglucosaminyltransferase deficiencies cause carbohydrate-deficient glycoprotein syndrome type II, underscoring the clinical relevance of this enzyme class. Studying GO:0047223 provides insight into glycan diversification and offers a target for glycoengineering and therapeutic development.
• Defines a key elongation step in mucin-type O-glycan biosynthesis, extending core 1-derived structures.
• Contributes to the structural diversity of O-glycans on secreted and membrane proteins, influencing protein function.
• Related glycosyltransferase deficiencies cause carbohydrate-deficient glycoprotein syndrome type II, a severe congenital disorder.
• Altered N-glycan processing, a parallel pathway, is observed in ocular autoimmune disease, highlighting links between glycosylation and inflammation.
• Enables glycoengineering of therapeutic proteins by controlling O-glycan branching.
• Provides a biochemical marker for distinguishing O-glycan from N-glycan biosynthetic enzymes.
• Supports research on host-pathogen interactions, as O-glycans are often exploited by pathogens.
• Facilitates the development of enzyme inhibitors or substrates for glycan analysis.
• Helps interpret glycomics data by assigning specific glycosyltransferase activities to observed glycan structures.
• Offers a basis for comparative glycobiology across species, as homologs exist in mammals and insects.
What Happens During beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity?
Substrate Recognition and Binding
In simple terms: The enzyme first grabs onto a specific sugar chain that already has a particular shape.
The enzyme recognizes a beta-D-galactosyl-1,3-(N-acetyl-D-glucosaminyl-1,6)-N-acetyl-D-galactosaminyl-R acceptor, which is typically a core 2 or core 3 type O-glycan structure on a glycoprotein. This acceptor specificity ensures that the enzyme acts only on O-glycosyl-glycoproteins and not on free oligosaccharides or N-glycans. The binding likely involves interactions with the galactose and the adjacent N-acetylgalactosamine (GalNAc) residues, as shown by kinetic studies using mucin-derived acceptors from swine trachea epithelium.
UDP-GlcNAc Donor Binding
In simple terms: The enzyme picks up a sugar building block called UDP-GlcNAc to transfer it.
The enzyme binds UDP-N-acetyl-D-glucosamine (UDP-GlcNAc) as the donor substrate. This nucleotide sugar serves as the activated form of GlcNAc, providing the energy for the transfer reaction. The binding of UDP-GlcNAc is essential for catalysis, and the enzyme likely has a conserved UDP-sugar binding domain typical of glycosyltransferases.
Catalytic Transfer and Linkage Formation
In simple terms: The enzyme attaches the GlcNAc sugar to the galactose using a specific chemical bond.
The enzyme catalyzes the transfer of GlcNAc from UDP-GlcNAc to the galactose residue of the acceptor, forming a beta-1,3 linkage. The reaction products are N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,6)-N-acetyl-D-galactosaminyl-R and UDP. This elongation step extends the O-glycan chain, creating a branch that can be further modified by other glycosyltransferases.
Role in O-Glycan Biosynthesis Pathway
In simple terms: This enzyme is one step in a assembly line that builds complex sugar trees on proteins.
The activity is part of the sequential biosynthesis of mucin-type O-glycans, which begins with the addition of GalNAc to serine or threonine residues and proceeds through elongation and branching. By adding a beta-1,3-linked GlcNAc, the enzyme contributes to the formation of core 2 and core 3 structures, which are precursors for more complex O-glycans. This step is distinct from N-glycan processing enzymes such as MGAT2, which act on different substrates.
Enzyme Source and Biochemical Properties
In simple terms: Scientists first found this enzyme in pig airways and studied its behavior in test tubes.
The enzyme was purified and characterized from swine trachea epithelium, where it was shown to have both beta-1,6-N-acetylglucosaminyltransferase and beta-1,3-N-acetylglucosaminyltransferase activities. The beta-1,3 activity specifically transfers GlcNAc to the galactose of Gal beta 3(GlcNAc beta 6)GalNAc-mucin acceptors. The enzyme requires divalent cations for optimal activity, a common feature of many glycosyltransferases.
Key Genes Involved in GO:0047223 beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity
The genes encoding beta-1,3-N-acetylglucosaminyltransferase activities are part of the large glycosyltransferase family; below are key genes and proteins relevant to GO:0047223 and related glycosylation pathways.
| Gene | Major Role | Research Relevance |
|---|---|---|
| B3GNT6 | Encodes a beta-1,3-N-acetylglucosaminyltransferase that forms core 3 O-glycans | Potential candidate for the activity described by GO:0047223; studied in mucin biosynthesis |
| B3GNT3 | Beta-1,3-N-acetylglucosaminyltransferase that elongates O-glycans | Related enzyme in O-glycan elongation; useful for comparative studies |
| B3GNT2 | Beta-1,3-N-acetylglucosaminyltransferase involved in poly-N-acetyllactosamine synthesis | Model for studying beta-1,3 linkage formation |
| MGAT2 | Alpha-1,6-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase II; acts on N-glycans | Deficiency causes CDG-II; distinct from GO:0047223 but shares N-acetylglucosaminyltransferase mechanism |
| MGAT1 | Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase I; N-glycan processing | Related glycosyltransferase for comparative enzymology |
| GALNT1 | Polypeptide N-acetylgalactosaminyltransferase 1; initiates O-glycosylation | Upstream of GO:0047223 in O-glycan pathway |
| GALNT2 | Polypeptide N-acetylgalactosaminyltransferase 2; initiates O-glycosylation | Provides substrate for elongation enzymes |
| C1GALT1 | Core 1 beta-1,3-galactosyltransferase; forms T antigen | Generates acceptor for GO:0047223 activity |
| C1GALT1C1 | Core 1 beta-1,3-galactosyltransferase chaperone | Regulates core 1 synthesis, affecting substrate availability |
| ST3GAL1 | Alpha-2,3-sialyltransferase; modifies O-glycans | Competes with elongation enzymes for acceptor |
| ST6GALNAC1 | Alpha-2,6-sialyltransferase; modifies O-glycans | Alternative modification of core 1 |
| B4GALT1 | Beta-1,4-galactosyltransferase 1; extends N- and O-glycans | Provides galactose acceptor for beta-1,3-GlcNAc transfer |
| B4GALT2 | Beta-1,4-galactosyltransferase 2 | Related galactosyltransferase |
| B3GALT1 | Beta-1,3-galactosyltransferase 1 | Forms beta-1,3 linkages on glycans |
| B3GALT2 | Beta-1,3-galactosyltransferase 2 | Related enzyme for glycan elongation |
| FUT2 | Fucosyltransferase 2; adds fucose to O-glycans | Downstream modification of O-glycans |
| FUT3 | Fucosyltransferase 3 | Modifies O-glycan termini |
| SLC35A2 | UDP-galactose transporter | Supplies nucleotide sugars for glycosylation |
How Is beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity Regulated?
The activity of beta-1,3-N-acetylglucosaminyltransferase is regulated at multiple levels, including enzyme expression, substrate availability, and nucleotide sugar transport. Inflammatory stress can alter N-glycan processing, as shown in ocular autoimmune disease, suggesting that glycosylation pathways are sensitive to inflammatory signals. The enzyme requires divalent cations for activity, and its kinetic properties can be modulated by the concentration of UDP-GlcNAc and acceptor substrates. Additionally, the expression of glycosyltransferases is often tissue-specific and developmentally regulated, contributing to the diversity of glycan structures.
beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| MGAT2 | Carbohydrate-deficient glycoprotein syndrome type II (CDG-II) | Knockout of MGAT2 in cell lines to study N-glycan processing; patient-derived fibroblasts |
| B3GNT6 | Mucin-type O-glycan biosynthesis; potential role in inflammation | Knockout and overexpression in intestinal epithelial cells |
| B3GNT3 | O-glycan elongation; implicated in cancer glycan remodeling | CRISPR knockout in cancer cell lines followed by glycomics |
| C1GALT1 | T-synthase deficiency (rare); O-glycan biosynthesis | Knockout in cell lines to block core 1 synthesis |
| GALNT1 | O-glycosylation initiation; potential role in autoimmunity | Overexpression and knockout in immune cells |
Carbohydrate-Deficient Glycoprotein Syndrome Type II (CDG-II)
Deficiency in N-acetylglucosaminyltransferase II (MGAT2), which catalyzes a related reaction on N-glycans, causes carbohydrate-deficient glycoprotein syndrome type II, an autosomal recessive disorder characterized by severe neurological and developmental abnormalities. Although GO:0047223 describes an O-glycan-specific activity, the clinical severity of MGAT2 deficiency underscores the importance of N-acetylglucosaminyltransferase enzymes in human health.
Inflammatory and Autoimmune Diseases
Altered glycosylation is a hallmark of inflammatory and autoimmune conditions. In ocular autoimmune disease, inflammatory stress causes N-glycan processing deficiency, indicating that glycosylation pathways are disrupted during inflammation. O-glycan elongation enzymes like the one described by GO:0047223 may similarly be affected, contributing to disease pathology.
Cancer and Glycan Remodeling
O-glycans are frequently remodeled in cancer, affecting cell adhesion, migration, and immune evasion. Although direct evidence for GO:0047223 in cancer is limited, the enzyme's role in elongating O-glycans suggests it could influence tumor-associated glycan structures. Further research using knockout and overexpression models is needed to clarify its contribution.
From beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Does loss of B3GNT6 alter O-glycan elongation? | B3GNT6 knockout cell line (e.g., HEK293 or intestinal epithelial cells) |
| Can a point mutation in the catalytic domain abolish transferase activity? | Point-mutation knock-in of catalytic residues in B3GNT6 |
| What is the effect of overexpressing the enzyme on glycan structures? | Overexpression of B3GNT6 or B3GNT3 in mammalian cells followed by mass spectrometry |
| Where is the enzyme localized within the cell? | Tagged knock-in with fluorescent protein (e.g., GFP) for imaging |
| Does the enzyme interact with other glycosyltransferases? | Knock-in of affinity tags (e.g., FLAG, HA) for co-immunoprecipitation |
| Can the enzyme be produced recombinantly for structural studies? | Heterologous expression in silkworm baculovirus or bacterial systems |
How to Study the beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Enzymatic assay with radiolabeled UDP-GlcNAc | Transferase activity and kinetics | Characterization of recombinant enzyme |
| Mass spectrometry glycomics | O-glycan structures and abundance | Profiling changes in knockout or overexpression cells |
| Heterologous expression in silkworm baculovirus | Production of active recombinant enzyme | Biochemical and structural studies |
| Bacterial expression system | Production of soluble active enzyme | Enzyme characterization |
| CRISPR-Cas9 knockout | Gene function loss | Studying O-glycan pathway |
| CRISPR-Cas9 knock-in | Tagged or mutant enzyme expression | Localization and interaction studies |
| Co-immunoprecipitation | Protein-protein interactions | Identifying glycosyltransferase complexes |
| Fluorescence microscopy | Subcellular localization | Determining Golgi localization |
Enzymatic Assays
The activity of beta-1,3-N-acetylglucosaminyltransferase can be measured using radiolabeled UDP-[3H]GlcNAc and defined acceptor substrates, followed by product separation by chromatography. Such assays are used to determine kinetic parameters and substrate specificity.
Glycomics and Mass Spectrometry
Mass spectrometry-based glycomics allows profiling of O-glycan structures in cells or tissues with altered enzyme expression. This method can reveal changes in core 2 and core 3 structures resulting from knockout or overexpression of the enzyme.
Heterologous Expression and Purification
Recombinant enzymes can be produced in silkworm baculovirus systems or bacterial expression systems for biochemical and structural studies. These systems enable the production of active glycosyltransferases for crystallization or kinetic analysis.
CRISPR-Cas9 Genome Editing
CRISPR-Cas9 knockout, point mutation, and knock-in strategies are used to dissect the function of glycosyltransferase genes in cell models. These approaches allow precise modification of candidate genes to study their role in O-glycan biosynthesis.
How CRISPR Can Be Used to Study GO:0047223 beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity
Knockout
CRISPR-Cas9 knockout of candidate glycosyltransferase genes such as B3GNT6 or B3GNT3 can abolish enzyme activity, allowing researchers to assess the contribution of GO:0047223 to O-glycan biosynthesis. Knockout cell lines are valuable for glycomics and functional assays.
Point Mutation
Introducing point mutations in the catalytic domain of the enzyme can help identify essential residues for transferase activity. Such models are useful for separating catalytic function from structural roles.
Knock-in
Knock-in of epitope tags or fluorescent proteins allows visualization and purification of the enzyme for interaction and localization studies. This approach can also be used to express mutant enzymes under endogenous regulatory control.
Overexpression
Overexpression of the enzyme in mammalian cells can enhance O-glycan elongation, providing a gain-of-function model to study downstream effects on cell behavior and glycan structure. Overexpression is also used to produce recombinant enzyme for biochemical assays.
How EDITGENE Supports beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity Research
Researchers studying beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity-related genes often need to determine whether a candidate gene is causally involved in O-glycan biosynthesis, inflammation, or cancer. EDITGENE provides comprehensive CRISPR-based services to create precise cell models for such investigations.
Contact EDITGENE today to design your custom CRISPR model for beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity research.
Frequently Asked Questions About beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity
What is GO:0047223?
GO:0047223 is a Gene Ontology molecular function term for beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity, which catalyzes the addition of GlcNAc to O-glycosyl-glycoprotein acceptors.
What reaction does beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase catalyze?
It transfers N-acetyl-D-glucosamine from UDP-GlcNAc to a beta-D-galactosyl-1,3-(N-acetyl-D-glucosaminyl-1,6)-N-acetyl-D-galactosaminyl-R acceptor, forming a beta-1,3 linkage and UDP.
What genes are involved in beta-1,3-N-acetylglucosaminyltransferase activity?
Genes such as B3GNT6, B3GNT3, and B3GNT2 encode enzymes with related beta-1,3-N-acetylglucosaminyltransferase activities, while MGAT2 encodes a distinct N-glycan-specific enzyme.
Which diseases are linked to defects in N-acetylglucosaminyltransferase activity?
Deficiency in MGAT2 causes carbohydrate-deficient glycoprotein syndrome type II, a severe congenital disorder; altered glycosylation is also seen in inflammatory and autoimmune diseases.
How is beta-1,3-N-acetylglucosaminyltransferase activity measured?
It is typically measured using enzymatic assays with radiolabeled UDP-GlcNAc and specific acceptor substrates, followed by product analysis.
What is the role of O-glycans in health and disease?
O-glycans are important for protein stability, cell adhesion, and immune recognition; their dysregulation is associated with inflammation, autoimmunity, and cancer.
Can CRISPR be used to study GO:0047223?
Yes, CRISPR-Cas9 knockout, point mutation, knock-in, and overexpression models can be used to dissect the function of glycosyltransferase genes related to GO:0047223.
What model systems are used to study beta-1,3-N-acetylglucosaminyltransferase?
Common models include mammalian cell lines, silkworm baculovirus expression systems, and bacterial expression systems for recombinant enzyme production.
Is GO:0047223 the same as MGAT2?
No, GO:0047223 describes an O-glycan-specific beta-1,3-N-acetylglucosaminyltransferase activity, whereas MGAT2 is a beta-1,2-N-acetylglucosaminyltransferase that acts on N-glycans.
Where can I find more information about GO:0047223?
Authoritative information is available from QuickGO, and biochemical details are described in studies on swine trachea epithelium and related enzymes.
Conclusion
GO:0047223 defines a specific glycosyltransferase activity that elongates O-glycans by adding beta-1,3-linked GlcNAc. This activity is part of the complex machinery that generates diverse O-glycan structures, which are critical for protein function and cell signaling. Although direct disease links are still emerging, related glycosyltransferase deficiencies cause severe congenital disorders, and altered glycosylation is a feature of inflammation and autoimmunity. Continued research using CRISPR models and glycomics will clarify the biological roles of this enzyme and its potential as a therapeutic target.
References
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- 3. Miyazaki T et al.. 2019. Expression and characterization of silkworm Bombyx mori β-1,2-N-acetylglucosaminyltransferase II, a key enzyme for complex-type N-glycan biosynthesis.. J Biosci Bioeng 127(3):273-280 PMID: 30253927
- 4. Charuk JH et al.. 1995. Carbohydrate-deficient glycoprotein syndrome type II. An autosomal recessive N-acetylglucosaminyltransferase II deficiency different from typical hereditary erythroblastic multinuclearity, with a positive acidified-serum lysis test (HEMPAS).. Eur J Biochem 230(2):797-805 PMID: 7607254
- 5. Kajiura H et al.. 2020. Characterization of Bombyx mori N-acetylglucosaminyltransferase II splicing variants.. Biochem Biophys Res Commun 529(2):404-410 PMID: 32703443
- 6. Miyazaki T et al.. 2018. Heterologous expression, purification and characterization of human β-1,2-N-acetylglucosaminyltransferase II using a silkworm-based Bombyx mori nucleopolyhedrovirus bacmid expression system.. J Biosci Bioeng 126(1):15-22 PMID: 29409697
- 7. Jaeken J et al.. 1994. Carbohydrate deficient glycoprotein syndrome type II: a deficiency in Golgi localised N-acetyl-glucosaminyltransferase II.. Arch Dis Child 71(2):123-7 PMID: 7944531
- 8. Sangadala S et al.. 1991. UDP-GlcNAc: Gal beta 3GalNAc-mucin: (GlcNAc----GalNAc) beta 6-N-acetylglucosaminyltransferase and UDP-GlcNAc: Gal beta 3(GlcNAc beta 6) GalNAc-mucin (GlcNAc----Gal)beta 3-N-acetylglucosaminyltransferase from swine trachea epithelium.. Mol Cell Biochem 101(2):125-43 PMID: 1830637
