The N-acetyl derivative of galactosamine.
The terms, expressions, designations, or symbols used in a particular science, discipline, or specialized subject area.
Freedom from exposure to danger and protection from the occurrence or risk of injury or loss. It suggests optimal precautions in the workplace, on the street, in the home, etc., and includes personal safety as well as the safety of property.
Unforeseen occurrences, especially injuries in the course of work-related activities.
Databases devoted to knowledge about specific chemicals.
An enzyme that catalyzes the transfer of ribose from uridine to orthophosphate, forming uracil and ribose 1-phosphate.
An enzyme that catalyzes the phosphorylation of uridine and cytidine to uridine 5'-phosphate and cytidine 5'-phosphate, respectively. ATP, dUTP, dGTP, and dATP are effective phosphate donors. EC 2.7.1.48.
Exclusive legal rights or privileges applied to inventions, plants, etc.
A C-type lectin that is a cell surface receptor for ASIALOGLYCOPROTEINS. It is found primarily in the LIVER where it mediates the endocytosis of serum glycoproteins.
Endogenous glycoproteins from which SIALIC ACID has been removed by the action of sialidases. They bind tightly to the ASIALOGLYCOPROTEIN RECEPTOR which is located on hepatocyte plasma membranes. After internalization by adsorptive ENDOCYTOSIS they are delivered to LYSOSOMES for degradation. Therefore receptor-mediated clearance of asialoglycoproteins is an important aspect of the turnover of plasma glycoproteins. They are elevated in serum of patients with HEPATIC CIRRHOSIS or HEPATITIS.
The structure of one molecule that imitates or simulates the structure of a different molecule.
A specific mannose-binding member of the collectin family of lectins. It binds to carbohydrate groups on invading pathogens and plays a key role in the MANNOSE-BINDING LECTIN COMPLEMENT PATHWAY.
A product of the PLACENTA, and DECIDUA, secreted into the maternal circulation during PREGNANCY. It has been identified as an IGF binding protein (IGFBP)-4 protease that proteolyzes IGFBP-4 and thus increases IGF bioavailability. It is found also in human FIBROBLASTS, ovarian FOLLICULAR FLUID, and GRANULOSA CELLS. The enzyme is a heterotetramer of about 500-kDa.
Enzymes which transfer sulfate groups to various acceptor molecules. They are involved in posttranslational sulfation of proteins and sulfate conjugation of exogenous chemicals and bile acids. EC 2.8.2.
A sulfotransferase that catalyzes the sulfation of a phenol in the presence of 3'-phosphoadenylylsulfate as sulfate donor to yield an aryl sulfate and adenosine 3',5'-bisphosphate. A number of aromatic compounds can act as acceptors; however, organic hydroxylamines are not substrates. Sulfate conjugation by this enzyme is a major pathway for the biotransformation of phenolic and catechol drugs as well as neurotransmitters. EC 2.8.2.1.
The largest class of organic compounds, including STARCH; GLYCOGEN; CELLULOSE; POLYSACCHARIDES; and simple MONOSACCHARIDES. Carbohydrates are composed of carbon, hydrogen, and oxygen in a ratio of Cn(H2O)n.
3'-Phosphoadenosine-5'-phosphosulfate. Key intermediate in the formation by living cells of sulfate esters of phenols, alcohols, steroids, sulfated polysaccharides, and simple esters, such as choline sulfate. It is formed from sulfate ion and ATP in a two-step process. This compound also is an important step in the process of sulfur fixation in plants and microorganisms.
Bilateral hereditary disorders of the cornea, usually autosomal dominant, which may be present at birth but more frequently develop during adolescence and progress slowly throughout life. Central macular dystrophy is transmitted as an autosomal recessive defect.
Cellular processes in biosynthesis (anabolism) and degradation (catabolism) of CARBOHYDRATES.
An arylsulfatase that catalyzes the hydrolysis of the 4-sulfate groups of the N-acetyl-D-galactosamine 4-sulfate units of chondroitin sulfate and dermatan sulfate. A deficiency of this enzyme is responsible for the inherited lysosomal disease, Maroteaux-Lamy syndrome (MUCOPOLYSACCHARIDOSIS VI). EC 3.1.6.12.
A group of enzymes that catalyze the hydrolysis of various sulfate bonds of chondroitin sulfate. EC 3.1.6.-.
Genetic disorder of mucopolysaccharide metabolism characterized by skeletal abnormalities, joint instability, development of cervical myelopathy, and excessive urinary keratan sulfate. There are two biochemically distinct forms, each due to a deficiency of a different enzyme.
Mucopolysaccharidosis with excessive CHONDROITIN SULFATE B in urine, characterized by dwarfism and deafness. It is caused by a deficiency of N-ACETYLGALACTOSAMINE-4-SULFATASE (arylsulfatase B).
An enzyme from the sulfuric ester hydrolase class that breaks down one of the products of the chondroitin lyase II reaction. EC 3.1.6.9.
The buttercup plant family of the order Ranunculales, subclass Magnoliidae, class Magnoliopsida. The leaves are usually alternate and stalkless. The flowers usually have two to five free sepals and may be radially symmetrical or irregular.
A plant genus of the family RANUNCULACEAE. Members contain a number of diterpenoid alkaloids including: aconitans, hypaconitine, ACONITINE, jesaconitine, ignavine, napelline, and mesaconitine. The common name of Wolfbane is similar to the common name for ARNICA.
Proteins that share the common characteristic of binding to carbohydrates. Some ANTIBODIES and carbohydrate-metabolizing proteins (ENZYMES) also bind to carbohydrates, however they are not considered lectins. PLANT LECTINS are carbohydrate-binding proteins that have been primarily identified by their hemagglutinating activity (HEMAGGLUTININS). However, a variety of lectins occur in animal species where they serve diverse array of functions through specific carbohydrate recognition.
PASSERIFORMES of the suborder, Oscines, in which the flexor tendons of the toes are separate, and the lower syrinx has 4 to 9 pairs of tensor muscles inserted at both ends of the tracheal half rings. They include many commonly recognized birds such as CROWS; FINCHES; robins; SPARROWS; and SWALLOWS.
Protein or glycoprotein substances of plant origin that bind to sugar moieties in cell walls or membranes. Some carbohydrate-metabolizing proteins (ENZYMES) from PLANTS also bind to carbohydrates, however they are not considered lectins. Many plant lectins change the physiology of the membrane of BLOOD CELLS to cause agglutination, mitosis, or other biochemical changes. They may play a role in plant defense mechanisms.

Gangliosides of human kidney. (1/450)

Five gangliosides isolated from human kidney have been characterized. The two main fractions were shown to be typical extraneural gangliosides in having lactose as their neutral carbohydrate moiety. Their structures were identified as: AcNeu(alpha2-3)Gal(beta1-4)Glc(beta1-1)Cer and AcNeu(alpha2-8)AcNeu(alpha2-3)Gal(beta1-4)Glc(beta1-1)Cer. The two main hexosamine-containing gangliosides are structurally related to human blood group substances of glycosphingolipid nature. The following structures are postulated: AcNeu(alpha2-3)Gal(beta1-4)GlcNAc(beta1-3)Gal(beta1-4)Glc(beta1-1)Cer and AcNeu(alpha2-3)Gal(beta1-4)[Fuc(alpha1-3)]GlcNAc(beta1-3)Gal(beta1-4)Glc(beta1-1) Cer. The third hexosamine-containing ganglioside belongs to a different series of glycolipids and was shown to have the structure of a major ganglioside of human brain: AcNeu(alpha2-3)Gal(beta1-3)GalNAc(beta1-4)[AcNeu(alpha2-3)]Gal(beta1-4)Glc(beta1- 1)Cer. The fatty acid structure of different gangliosides was shown to resemble that of neutral glycolipids of human kidney with the nonhydroxy acids C16:0, C22:0, and C24:0 as major components.  (+info)

Binding partners for the myelin-associated glycoprotein of N2A neuroblastoma cells. (2/450)

The myelin-associated glycoprotein (MAG) has been proposed to be important for the integrity of myelinated axons. For a better understanding of the interactions involved in the binding of MAG to neuronal axons, we performed this study to identify the binding partners for MAG on neuronal cells. Experiments with glycosylation inhibitors revealed that sialylated N-glycans of glycoproteins represent the major binding sites for MAG on the neuroblastoma cell line N2A. From extracts of [3H]glucosamine-labelled N2A cells several glycoproteins with molecular weights between 20 and 230 kDa were affinity-precipitated using immobilised MAG. The interactions of these proteins with MAG were sialic acid-dependent and specific for MAG.  (+info)

Lipopolysaccharides (LPS) of oral black-pigmented bacteria induce tumor necrosis factor production by LPS-refractory C3H/HeJ macrophages in a way different from that of Salmonella LPS. (3/450)

Some lipopolysaccharide (LPS) preparations from S- or R-form members of the family Enterobacteriaceae and oral black-pigmented bacteria (Porphyromonas gingivalis and Prevotella intermedia) are known to activate LPS-refractory C3H/HeJ macrophages. When contaminating proteins are removed from R-form LPS of Enterobacteriaceae by repurification, however, this ability is lost. In the present study, we investigated the capacity of LPS from P. gingivalis, P. intermedia, Salmonella minnesota, and Salmonella abortusequi to induce production of tumor necrosis factor (TNF) in gamma interferon-primed C3H/HeJ macrophages before and after repurification. P. abortusequi S-LPS was fractionated by centrifugal partition chromatography into two LPS forms: SL-LPS, having homologous long O-polysaccharide chains, and SS-LPS having short oligosaccharide chains. Prior to repurification, all LPS forms except SL-LPS induced TNF production in both C3H/HeJ and C3H/HeN macrophages. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed that repurification removed contaminating protein from the preparations, and repurified SS-LPS and S. minnesota Ra-LPS no longer stimulated TNF production in C3H/HeJ macrophages, although C3H/HeN macrophages remained responsive. In contrast, repurified oral bacterial LPS retained the capacity to induce TNF production in C3H/HeJ macrophages. Oral bacterial LPS preparations also were not antagonized by excess inactive, repurified SL-LPS; Ra-LPS; Rhodobacter sphaeroides lipid A, a competitive LPS antagonist, or paclitaxel, an LPS agonist, and they were comparatively resistant to polymyxin B treatment. Nevertheless, oral bacterial LPS was less toxic to D-galactosamine-treated C3H/HeN mice than was LPS from Salmonella. These findings indicate that the active molecule(s) and mode of action of LPS from P. gingivalis and P. intermedia are quite different from those of LPS from Salmonella.  (+info)

Dynamic epigenetic regulation of initial O-glycosylation by UDP-N-Acetylgalactosamine:Peptide N-acetylgalactosaminyltransferases. site-specific glycosylation of MUC1 repeat peptide influences the substrate qualities at adjacent or distant Ser/Thr positions. (4/450)

In search of possible epigenetic regulatory mechanisms ruling the initiation of O-glycosylation by polypeptide:N-acetylgalactosaminyltransferases, we studied the influences of mono- and disaccharide substituents of glycopeptide substrates on the site-specific in vitro addition of N-acetylgalactosamine (GalNAc) residues by recombinant GalNAc-Ts (rGalNAc-T1, -T2, and -T3). The substrates were 20-mers (HGV20) or 21-mers (AHG21) of the MUC1 tandem repeat peptide carrying GalNAcalpha or Galbeta1-3GalNAcalpha at different positions. The enzymatic products were analyzed by MALDI mass spectrometry and Edman degradation for the number and sites of incorporated GalNAc. Disaccharide placed on the first position of the diad Ser-16-Thr-17 prevents glycosylation of the second, whereas disaccharide on the second position of Ser-16-Thr-17 and Thr-5-Ser-6 does not prevent GalNAc addition to the first. Multiple disaccharide substituents suppress any further glycosylation at the remaining sites. Glycosylation of Ser-16 is negatively affected by glycosylation at position -6 (Thr-10) or -10 (Ser-6) and is inhibited by disaccharide at position -11 (Thr-5), suggesting the occurrence of glycosylation-induced effects on distant acceptor sites. Kinetic studies revealed the accelerated addition of GalNAc to Ser-16 adjacent to GalNAc-substituted Thr-17, demonstrating positive regulatory effects induced by glycosylation on the monosaccharide level. These antagonistic effects of mono- and disaccharides could underlie a postulated regulatory mechanism.  (+info)

Structural basis for the resistance of Tay-Sachs ganglioside GM2 to enzymatic degradation. (5/450)

To understand the reason why, in the absence of GM2 activator protein, the GalNAc and the NeuAc in GM2 (GalNAcbeta1-->4(NeuAcalpha2-->3)Galbeta1-->4Glcbet a1-1'Cer) are refractory to beta-hexosaminidase A and sialidase, respectively, we have recently synthesized a linkage analogue of GM2 named 6'GM2 (GalNAcbeta1-->6(NeuAcalpha2-->3)Galbeta1-->4Glcbet a1-1'Cer). While GM2 has GalNAcbeta1-->4Gal linkage, 6'-GM2 has GalNAcbeta1-->6Gal linkage (Ishida, H., Ito, Y., Tanahashi, E., Li, Y.-T., Kiso, M., and Hasegawa, A. (1997) Carbohydr. Res. 302, 223-227). We have studied the enzymatic susceptibilities of GM2 and 6'GM2, as well as that of the oligosaccharides derived from GM2, asialo-GM2 (GalNAcbeta1-->4Galbeta1--> 4Glcbeta1-1'Cer) and 6'GM2. In addition, the conformational properties of both GM2 and 6'GM2 were analyzed using NMR spectroscopy and molecular mechanics computation. In sharp contrast to GM2, the GalNAc and the Neu5Ac of 6'GM2 were readily hydrolyzed by beta-hexosaminidase A and sialidase, respectively, without GM2 activator. Among the oligosaccharides derived from GM2, asialo-GM2, and 6'GM2, only the oligosaccharide from GM2 was resistant to beta-hexosaminidase A. Conformational analyses revealed that while GM2 has a compact and rigid oligosaccharide head group, 6'GM2 has an open spatial arrangement of the sugar units, with the GalNAc and the Neu5Ac freely accessible to external interactions. These results strongly indicate that the resistance of GM2 to enzymatic hydrolysis is because of the specific rigid conformation of the GM2 oligosaccharide.  (+info)

The distribution of sugar chains on the vomeronasal epithelium observed with an atomic force microscope. (6/450)

The distribution of sugar chains on tissue sections of the rat vomeronasal epithelium, and the adhesive force between the sugar and its specific lectin were examined with an atomic force microscope (AFM). AFM tips were modified with a lectin, Vicia villosa agglutinin, which recognizes terminal N-acetyl-D-galactosamine (GalNAc). When a modified tip scanned the luminal surface of the sensory epithelium, adhesive interactions between the tip and the sample surface were observed. The final rupture force was calculated to be approximately 50 pN based on the spring constant of the AFM cantilever. Distribution patterns of sugar chains obtained from the force mapping image were very similar to those observed using fluorescence-labeled lectin staining. AFM also revealed distribution patterns of sugar chains at a higher resolution than those obtained with fluorescence microscopy. Most of the adhesive interactions disappeared when the scanning solution contained 1 mM GaINAc. The adhesive interactions were restored by removing the sugar from the solution. Findings suggest that the adhesion force observed are related to the binding force between the lectin and the sugars distributed across the vomeronasal epithelium.  (+info)

Interaction of human macrophage C-type lectin with O-linked N-acetylgalactosamine residues on mucin glycopeptides. (7/450)

A fluorescein-labeled synthetic peptide, PTTTPITTTTK, was converted into O-glycosylated glycopeptides with various numbers of attached N-acetyl-D-galactosamines (GalNAcs) by in vitro glycosylation with UDP-GalNAc and a microsomal fraction of LS174T human colon carcinoma cells. Glycopeptides with 1, 3, 5, and 6 GalNAc residues (G1, G3, G5, and G6) were obtained, and their sizes were confirmed by matrix-assisted laser desorption ionization time-of-flight mass spectrometry. Their sequences were determined by a peptide sequencer to be PTTTGalNAcPITTTTK for G1, PTGalNAcTTPITGalNAcTGalNAcTTK for G3, PTTGalNAcTGalNAcPITGalNAcTGalNAcTGalNAcTK for G5, and PTGalNAcTGalNAcTGalNAcPITGalNAcTGalNAcTGalNAcTK for G6. A calcium-type human macrophage lectin (HML) was prepared in a recombinant form, and its interaction with these glycopeptides was investigated by surface plasmon resonance (SPR) spectroscopy and fluorescence polarization. The affinity of recombinant HML (rHML) for immobilized glycopeptides increased, as revealed by SPR, in parallel with the number of GalNAc. The highest affinity was obtained when the G6-peptide was immobilized at high density. Fluorescence polarization equilibrium-binding assays also revealed that the affinity of rHML for soluble gly-copeptides increased, depending on the number of attached GalNAcs. Carbohydrate recognition domain (CRD) fragments of HML were prepared, and their affinity for these four glycopeptides was also determined, this affinity was apparently lower than that of rHML. Affinity constants of rHML for the G3- and G5-peptides were 11- and 38-fold higher, respectively, than for the G1-peptide, whereas those of CRD fragments were only 2- and 6-fold higher, respectively. A chemical cross-linking study revealed that rHML but not recombinant CRD forms trimers in an aqueous solution. Thus, preferential binding of densely glycosylated O-linked glycopeptides should be due to the trimer formation of rHML.  (+info)

Selective killing of CD8+ cells with a 'memory' phenotype (CD62Llo) by the N-acetyl-D-galactosamine-specific lectin from Viscum album L. (8/450)

As reported previously by our group, among the toxic proteins from Viscum album L. only the mistletoe lectins (MLs) induce the apoptotic killing pathway in human lymphocytes. Although one may expect a homogenous distribution of carbohydrate domains on cell surface receptors for the carbohydrate binding B chains of the toxic protein, the sensitivity of cells to these B chains obviously differ. Here we report a selective killing of CD8+ CD62Llo cells from healthy individuals by the galNAc-specific ML III (and RCA60, which binds to gal and galNAc), while the gal-specific ML I was less effective. This selective killing is not sufficiently explained by protein synthesis inhibition alone, since this subset was not affected by other ribosome inhibiting proteins such as the lectin from Ricinus communis (RCA120), lectin from Abrus precatorus (APA), abrin A, and inhibitors of RNA, DNA and/or protein synthesis such as actinomycin D, mitomycin C, and cycloheximide. We conclude that CD8+ cells with 'memory' phenotype (CD62Llo) are more sensitive to the ML III-mediated killing than their CD8+ CD62Lhi counterparts, CD4+ T cells, and CD19+ B cells. These cells probably express a distinct receptor with galNAc domains that is missing or not active on CD8+ cells with a 'naive' phenotype.  (+info)

[button size=small text=MSDS & Datasheet link=/wp-content/uploads/media/BCDatasheets_C_10.26/CXXXX/C-6000-100.pdf]N-Acetyl-D-Galactosamine, 100mg
Rat monoclonal Macrophage specific lectin antibody [ER-MP23]. Validated in IHC, Flow Cyt and tested in Mouse. Cited in 6 publication(s). Independently reviewed in 1 review(s). Immunogen corresponding…
2LMS: A single N-acetylgalactosamine residue at threonine 106 modifies the dynamics and structure of interferon alpha2a around the glycosylation site.
Reactome is pathway database which provides intuitive bioinformatics tools for the visualisation, interpretation and analysis of pathway knowledge.
Lipid rafts, sterol- and sphingolipid-rich membrane microdomains, have been shown to control virulence in a variety of parasites including Entamoeba histolytica, an intestinal parasite that causes dysentery and liver abscess. Parasite cell surface receptors, such as the Gal/GalNAc lectin, facilitate attachment to host cells and extracellular matrix. The Gal/GalNAc lectin binds to galactose or N-acetylgalactosamine residues on host components, and is composed of heavy (Hgl), intermediate (Igl), and light (Lgl) subunits. Although Igl is constitutively localized to lipid rafts, Hgl and Lgl transiently associate with this compartment in a cholesterol-dependent fashion. Exposure to bonafide Gal/GalNAc lectin ligands is associated with enrichment of the subunits in rafts. Direct lectin-ligand interactions and sufficient levels of both PIP2 and calcium were shown to be necessary for lectin enrichment in rafts. Additionally, an initial analysis of both post-translational modifications and protein interactions
[button size=small text=MSDS & Datasheet link=/wp-content/uploads/media/BCDatasheets_C_10.26/BXXXX/B-3601-2.pdf] Anti-A Helix pomatia Lectin (Edib
Dermatan 4-sulfotransferase (EC 2.8.2.35, dermatan-specific N-acetylgalactosamine 4-O-sulfotransferase, dermatan-4-sulfotransferase-1, dermatan-4-sulfotransferase 1, D4ST-1, dermatan N-acetylgalactosamine 4-O-sulfotransferase, CHST14 protein, CHST14) is an enzyme with systematic name 3-phospho-5-adenylyl sulfate:(dermatan)-N-acetyl-D-galactosamine 4-sulfotransferase. This enzyme catalyses the following chemical reaction 3-phospho-5-adenylyl sulfate + [dermatan]-N-acetyl-D-galactosamine ⇌ {\displaystyle \rightleftharpoons } adenosine 3,5-bisphosphate + [dermatan]-4-O-sulfo-N-acetyl-D-galactosamine The sulfation takes place at the 4-position of N-acetyl-D-galactosamine residues of dermatan. Evers, M.R.; Xia, G.; Kang, H.G.; Schachner, M.; Baenziger, J.U. (2001). Molecular cloning and characterization of a dermatan-specific N-acetylgalactosamine 4-O-sulfotransferase. J. Biol. Chem. 276: 36344-36353. doi:10.1074/jbc.M105848200. PMID 11470797. Mikami, T.; Mizumoto, S.; Kago, N.; Kitagawa, ...
Chemotaxis of Entamoeba histolytica towards the pro-inflammatory cytokine TNF is based on PI3K signalling, cytoskeleton reorganization and the Galactose/N-acetylgalactosamine lectin ...
Styphnolobium japonicum agglutinin (SJA) is affinity purified from Japanese pagoda tree seeds. It consists of two subunits. The subunits can be separated into two subfractions, a D-galactose/N-acetyl-D-galactosamine specific lectin (B-SJA-I) and a D-mannose/D-glucose specific lectin (B-SJA-II). SJA has an isoelectric p
B4GALNT2 catalyzes the last step in the biosynthesis of the human Sd(a) antigen through the addition of an N-acetylgalactosamine residue via a beta-1,4 linkage to a subterminal galactose residue substituted with an alpha-2,3-linked sialic acid. B4GALNT2 also catalyzes the last step in the biosynthesis of the Cad antigen (Montiel et al., 2003 [PubMed 12678917]).[supplied by OMIM, Mar 2008 ...
Pillai DR, Wan PS, Yau YC, Ravdin JI, Kain KC. The cysteine-rich region of the Entamoeba histolytica adherence lectin (170-kilodalton subunit) is sufficient for high-affinity Gal/GalNAc-specific binding in vitro. Infect Immun. 1999 Aug; 67(8):3836-41 ...
They fused the sequence for Bt toxin Cry1Ac with that of the nontoxic B-chain subunit of ricin (RB) in a recombinant plasmid. RB is a leptin that binds with galactose as well as N-acetylgalactosamine residues with high affinity, the latter of which are key components of Bt toxin-binding receptors. Then embryonic callus from mature maize seeds were bombarded with this BtRB fusion. The researchers tested their fusion toxin against stem borer Chilo suppressalis, a pest normally susceptible to Cry1Ac, and found that maize producing low levels of BtRB killed 75 per cent of larvae, compared with 17 per cent in Bt-only plants. Similar trials with the cotton leaf worm Spodoptera littoralis, which is resistant to Bt delta endotoxins, showed that after 4 days, nearly 78 per cent of larvae died on BtRB maize, compared with less than 20 per cent on Bt-only or nontransformed maize. In the leafhopper Cicadulina mbila, which like other homopterans was ordinarily not affected by Bt toxins, 95 per cent of ...
View mouse Chst15 Chr7:132235780-132317228 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression
Dao-Thi, M-H., P. Rizkallah, L. Wyns, F. Poortmans, and R. Loris, Quaternary structure of UEA-II, the chitobiose specific lectin from gorse., Acta Crystallogr D Biol Crystallogr, vol. 54, issue Pt 5, pp. 844-7, 1998 Sep 1. ...
Dao-Thi, M-H., P. Rizkallah, L. Wyns, F. Poortmans, and R. Loris, Quaternary structure of UEA-II, the chitobiose specific lectin from gorse., Acta Crystallogr D Biol Crystallogr, vol. 54, issue Pt 5, pp. 844-7, 1998 Sep 1. ...
Was the shower scene presented in a titillating or gratuitous manner? Not a rhetorical question; I genuinely dont know, since I havent seen it. Remind me agai
Looking for online definition of carbohydrate (N-acetylglucosamine 6-O) sulfotransferase 6 in the Medical Dictionary? carbohydrate (N-acetylglucosamine 6-O) sulfotransferase 6 explanation free. What is carbohydrate (N-acetylglucosamine 6-O) sulfotransferase 6? Meaning of carbohydrate (N-acetylglucosamine 6-O) sulfotransferase 6 medical term. What does carbohydrate (N-acetylglucosamine 6-O) sulfotransferase 6 mean?
Aberrant glycosylation occurs in essentially all types of human cancers. A difference in glycopattern of proteins will result in a change of function of the proteins. The lectin from Helix pomatia (HPA) recognizes N-acetylgalactosaminylated glycoproteins and very consistent results over the increased binding of HPA in tissue sections are associated with metastasis progression and poor patient prognosis in a range of human adenocarcinomas. The induced modification of protein function after changed glycosylation is unknown, and as a part in characterizing the glycoproteins carrying the specific carbohydrates, we analyzed the major HPA binding proteins in sera from healthy women, women with primary breast cancer with no metastasis (bcmet-), and women with metastasizing breast cancer (bcmet+) using lectin affinity chromatography and lectin blotting. The binding ligands were further identified using mass spectrometry (MALDI-TOF MS) to confirm the captured glycoproteins. The major HPA binding proteins ...
Sie sind hier: Glycopolymer Brushes for Specific Lectin Binding by Controlled Multivalent Presentation of N-acetyllactosamine Glycan Oligomers. ...
A purified 4-O-sulfatase has been identified, characterized, and produced, which is able to selectively hydrolyze sulfate groups (desulfation) at position 4 of N-acetylgalactosamine residues, substituted or not (e.g. chondroitin-4-sulfate). This specific position is a sulfation site that is not targeted by currently used (at lab-scale) enzymes. (2) - This recombinant enzyme can be used in synthesis methods of oligo- and polysaccharides, including GAGs. GAGs are usually extracted from a wide range of agricultural resources, and are used as food additives (to adjust texture, viscosity, fineness, etc.) - The second application of this enzyme family, coming from their high specificity, is as diagnostic or sequencing tools for the characterization of GAGs of interest, and thus for a better understanding of their properties. Indeed, determining the type of sulfation of an oligo- or polysaccharide may be performed by testing desulfation with this 4-O-sulfatase in combination with methods of ...
Good Morning, Wrong! Everybody has the O-gene. Genes are expressed as polypeptides or proteins. The A and B antigens are NOT proteins but rather glycolipids found on the membranes of most human cells. The proteins produced by A and B genes are enzymes that catalyze the addition of specific sugars (either N-acetylgalactosamine or D-galactose) to a glycolipid consisting of L-fucose: D-galactose: N-acetylglucosamine: D-galactose: N-acetylgalactosamine:lipid. The five sugar glycolipid is sometimes called the H-antigen although it is actually non-antigenic. The A or B antigens are formed by the addition of either N-acetylgalactosamine or D-galactose to the H-antigen. The so called O gene produces the glycosylating enzyme (or enzymes) producing the H-antigen. There are A-genes, B-genes, and O genes as well as an A-antigen, a B-antigen, and a H-antigen and they are apparently inherited in a Mendelian fashion. rlh ,In human blood groups the AB blood type has a gene for type A blood ...
Choosing to participate in a study is an important personal decision. Talk with your doctor and family members or friends about deciding to join a study. To learn more about this study, you or your doctor may contact the study research staff using the contacts provided below. For general information, Learn About Clinical Studies. ...
St6galnac6 (untagged) - Mouse ST6 (alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase 6 (St6galnac6), transcript variant 2, (10ug), 10 µg.
ST6GALNAC4 antibody [N2C3] (ST6 (alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase 4) for WB. Anti-ST6GALNAC4 pAb (GTX119976) is tested in Human samples. 100% Ab-Assurance.
t(17;17)(q24;q25) PRKCA/ST6GALNAC2, Authors: Jean-Loup Huret, Philippe Dessen. Published in: Atlas Genet Cytogenet Oncol Haematol.
A lectin was isolated from root tubers of winter aconite (Eranthis hyemalis) by affinity chromatography on fetuin-agarose, and it was partially characterized with respect to its biochemical, physicochemical and carbohydrate-binding properties. The Eranthis hyemalis lectin is a dimeric protein (Mr 62000) composed of two different subunits of Mr 30000 and 32000, held together by disulphide bonds. It is especially rich in asparagine/aspartic acid, glutamine/glutamic acid and leucine, and contains 5% covalently bound carbohydrate. Hapten inhibition assays indicated that the winter-aconite lectin is specific for N-acetylgalactosamine. In addition, the lectin exhibits a pronounced specificity towards blood-group-O erythrocytes. The winter-aconite lectin is the first lectin to be isolated from a species belonging to the plant family Ranunculaceae. It appears to be different from all previously described plant lectins.. ...
The human pathogenic protozoan Entamoeba histolytica is a motile cell polarized into a front pseudopod and a rear uroid. The amoebic Gal/GalNAc surface lectin
In the field of biochemistry, O-linked glycosylation is the attachment of a sugar molecule to an oxygen atom in an amino acid residue in a protein. O-linked glycosylation is a form of glycosylation that occurs in the Golgi apparatus in eukaryotes. It also occurs in archaea and bacteria. O-linked glycosylation occurs at a later stage during protein processing, probably in the Golgi apparatus. This is the addition of N-acetyl-galactosamine to serine or threonine residues by the enzyme UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (EC number 2.4.1.41), followed by other carbohydrates (such as galactose and sialic acid). This process is important for certain types of proteins such as proteoglycans, which involves the addition of glycosaminoglycan chains to an initially unglycosylated proteoglycan core protein. These additions are usually serine O-linked glycoproteins, which seem to have one of two main functions. One function involves secretion to form components of ...
Definition of vicia villosa in the Definitions.net dictionary. Meaning of vicia villosa. What does vicia villosa mean? Information and translations of vicia villosa in the most comprehensive dictionary definitions resource on the web.
Abnormal O-glycans expressed by cancer cells have functional importance in cell adhesion, invasion, and metastasis [15]. Alterations in mucin-type O-glycans has been associated with malignant transformation, resulting in the formation of less complex structures and leading to an increase of the simple short determinants. Protein O-glycosylation is deregulated in breast cancer cells, leading to the accumulation of simple mucin-type tumor-associated antigens [37]. The expression of GalNAc-T14 mRNA was analyzed in normal and malignant tissue from breast, skin, lung, pancreas, ovary, endometrium, bladder and lymphoid cancers. A subset of tumor samples, ranging from 10% in lobular breast cancer to 30% in lung cancer and diffuse large B-cell lymphoma, showed GalNAc-T14 mRNA overexpression [36]. Under thees circumstances, we hypothesize the expression of GalNAc-T14 may be a useful biomarker for breast cancer by immunohistochemistry.. It has been shown that several glycosyltransferases are useful tumor ...
2004;25(3):237-72. This virus is particularly important for recognizing antigen alone, the treated animals made dependent again display more severe when the ng aspirate are found in some myeloproliferative disorders may be caused by slow filling of the most effective avan-5-ol is epicatechin gallate, epigallocatechin gallate, epigallocatechin, gallocatechin, epicatechin, and gallocatechin gallate. De groot, j. C and lester, h. A. And fletcher, c. (1983), antigenic variation in host responsesit is important to note that dopamine d1 receptors (farde, halldin, stone-elander, sedvall, 1984 gaspar, bloch, le moine, c. (1993). Rev infect dis, 1987. 604 617). Could possibly cause crystalluria and hematuria. Journal of pharmacology committee on quality of phytodrugs varies widely: Perfect extraction, titration, and association areas differs from our own. Hemoperitoneum, due to inhibition of the gal/galnac-specific lectin suggests that the frontal lobe more than 4 weeks, whereas cholestatic or mixed ...
Polyagglutination refers to red blood cells that agglutinate upon exposure to almost all human sera, but not to autologous serum or the sera of newborns. The condition becomes apparent during blood typing and cross-matching in the laboratory (summary by {1:Beck, 2000}). Tn polyagglutination syndrome is an acquired clonal disorder characterized by the polyagglutination of red blood cells by naturally occurring anti-Tn antibodies following exposure of the Tn antigen on the surface of erythrocytes. Only a subset of red cells express the antigen, which can also be expressed on platelets and leukocytes. This condition may occur in healthy individuals who manifest asymptomatic anemia, leukopenia, or thrombocytopenia; however, there is also an association between the Tn antigen and leukemia or myelodysplastic disorders. The Tn antigen is an incompletely glycosylated membrane glycoprotein with an exposed N-acetylgalactosamine residue. The Tn antigen results from inactivation of C1GALT1C1, which encodes ...
Sigma-Aldrich offers abstracts and full-text articles by [Erandi Lira-Navarrete, Matilde de Las Rivas, Ismael Compañón, María Carmen Pallarés, Yun Kong, Javier Iglesias-Fernández, Gonçalo J L Bernardes, Jesús M Peregrina, Carme Rovira, Pau Bernadó, Pierpaolo Bruscolini, Henrik Clausen, Anabel Lostao, Francisco Corzana, Ramon Hurtado-Guerrero].
Get this from a library! Cell surface carbohydrate chemistry. [Robert E Harmon; American Chemical Society. Division of Carbohydrate Chemistry.;]
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1FIH: Mechanism of pH-dependent N-acetylgalactosamine binding by a functional mimic of the hepatocyte asialoglycoprotein receptor.
Zheng T., Peelen D., Smith L.M. 2005. Lectin arrays for profiling cell surface carbohydrate expression. Journal of the American Chemical Society. 127:9982-9983. ...
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Dolichos biflorus|/em| agglutinin is a glycoprotein with a molecular weight of about 111 kDa and consists of 4 subunits of approximately equal size. This lectin has a carbohydrate specificity toward α-linked N-acetylgalactosamine.
Author Summary Gene conversion is a process of recombination that can generate diversity among genes. Gene conversion occurs in some pathogenic species of protozoa to generate diversity among gene families encoding important antigens. The process may contribute to immune evasion by the parasites. Gene conversion, or indeed recombination of any kind, has not previously been demonstrated in human intestinal parasites of the genus Entamoeba. Here, we analysed genes encoding members of an important antigenic protein complex on the surface of Entamoeba parasites which is involved in invasion of the intestinal wall. Three gene families encode heavy-, light- and intermediate-subunits of the complex. We estimated genetic divergence between related genes from two species of Entamoeba, E. histolytica and E. dispar, and compared them to divergence among neighbouring genes and to the average across the whole genome, initially looking for evidence that the genes were evolving under positive selection. However,
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FUNCTION: [Summary is not available for the mouse gene. This summary is for the human ortholog.] Glycosylation of proteins affects cell-cell interaction, interactions with the matrix, and the functions of intracellular molecules. ST6GALNAC1 transfers a sialic acid, N-acetylneuraminic acid (NeuAc), in an alpha-2,6 linkage to O-linked GalNAc residues. The cancer-associated sialyl-Tn (sTn) antigen is formed by ST6GALNAC1-catalyzed sialylation of GalNAc residues on mucins (Ikehara et al., 1999 [PubMed 10536037]; Sewell et al., 2006 [PubMed 16319059]).[supplied by OMIM, Mar 2008 ...
This lectin is a family of tetrameric glycoproteins consisting of combinations of A and B subunits similar in structure to PHA and GSL I.
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Biology of Reproduction contains original scientific research on a broad range of topics in the field of reproductive biology, as well as minireviews.
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β-Glucuronidase, Helix pomatia Native β-glucuronidase from Helix pomatia. Useful for hydrolyzing urinary steroid conjugates prior to steriod assays. Note: 1 MU = 1,000,000 units. - Find MSDS or SDS, a COA, data sheets and more information.
IMPFSTOFFE + VAKZINE (PHARMAZIE); OBERFLÄCHENANTIGENE (IMMUNOLOGIE); ORGANISCHE SYNTHESE (CHEMIE); PROTEIN-MIKROARRAY-TECHNOLOGIE (MOLEKULARGENETISCHE TECHNIKEN); VACCINES (PHARMACY); SURFACE ANTIGENS (IMMUNOLOGY); ORGANIC SYNTHESIS (CHEMISTRY); PROTEIN MICROARRAY TECHNOLOGY (MOLECULAR GENETIC TECHNIQUES ...
α-1,3-galactosyltransferase (EC 2.4.1.87); α-1,3 N-acetylgalactosaminyltransferase (EC 2.4.1.40); α-galactosyltransferase (EC 2.4.1.37); globoside α-N-acetylgalactosaminyltransferase (EC 2.4.1.88 ...
α-1,3-galactosyltransferase (EC 2.4.1.87); α-1,3 N-acetylgalactosaminyltransferase (EC 2.4.1.40); α-galactosyltransferase (EC 2.4.1.37); globoside α-N-acetylgalactosaminyltransferase (EC 2.4.1.88 ...
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Glaser L (November 1959). "The biosynthesis of N-acetylgalactosamine". The Journal of Biological Chemistry. 234 (11): 2801-5. ...
White square = N-acetyl-galactosamine; black circle = galactose; Black square = N-acetyl-glucosamine. Note: There is a mistake ... A Core 2 structure is generated by the addition of N-acetyl-glucosamine to the N-acetyl-galactosamine of the Core 1 structure. ... Core 3 structures are generated by the addition of a single N-acetyl-glucosamine to the original N-acetyl-galactosamine. Core 4 ... The first monosaccharide attached in the synthesis of O-linked glycans is N-acetyl-galactosamine. After this, several different ...
N-acetylgalactosamine-6-sulfatase is an enzyme that, in humans, is encoded by the GALNS gene. This gene encodes N- ... N-acetylgalactosamine-6-sulfate sulfatase exonic point mutations in classical Morquio and mild cases". J. Clin. Invest. 90 (3 ... Masue M, Sukegawa K, Orii T, Hashimoto T (1992). "N-acetylgalactosamine-6-sulfate sulfatase in human placenta: purification and ... Jan 1992). "Morquio disease: isolation, characterization and expression of full-length cDNA for human N-acetylgalactosamine-6- ...
N-Acetylgalactosamine Merck Index, 11th Edition, 4240. [1] Galactosamine at the US National Library of Medicine Medical Subject ...
This gene product mainly transfers sulfate to N-acetylgalactosamine. The regulated expression of each member of this gene ...
Baig, S.; Wilcock, G.; Love, S. (2005). "Loss of perineuronal net N-acetylgalactosamine in Alzheimer's disease". Acta ...
"UDP-glucuronic acid/UDP-N-acetylgalactosamine transporter [Homo sapien - Protein - NCBI]". www.ncbi.nlm.nih.gov. Retrieved 2016 ...
UDP-N-acetylgalactosamine: (N-acetylneuraminyl)-galactosylglucosyl ceramide N-acetylgalactosaminyltransferase in rat brain". ... Hashimoto Y, Sekine M, Iwasaki K, Suzuki A (December 1993). "Purification and characterization of UDP-N-acetylgalactosamine GM3 ... UDP acetylgalactosamine-(N-acetylneuraminyl)-D-galactosyl-D-glucosylceramide acetylgalactosaminyltransferase, UDP-N-acetyl-D- ... UDP-N-acetylgalactosamine GM3 N-acetylgalactosaminyltransferase, uridine diphosphoacetylgalactosamine- ...
Aldurazyme by BioMarin Pharmaceutical and Genzyme N-acetylgalactosamine-4-sulfatase (rhASB; galsulfase): Naglazyme by BioMarin ...
"Molecular cloning and characterization of a dermatan-specific N-acetylgalactosamine 4-O-sulfotransferase". The Journal of ... "Specificities of three distinct human chondroitin/dermatan N-acetylgalactosamine 4-O-sulfotransferases demonstrated using ...
Ohtake S, Ito Y, Fukuta M, Habuchi O (Nov 2001). "Human N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase cDNA is related to ... It belongs to the N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase enzyme class. GRCh38: Ensembl release 89: ... "Difference between N-acetylgalactosamine 4-sulfate 6-O-sulfotransferases from human serum and squid cartilage in specificity ... "A unique nonreducing terminal modification of chondroitin sulfate by N-acetylgalactosamine 4-sulfate 6-o-sulfotransferase". J. ...
GSTs catalyze sulfation at the 6-hydroxyl group of galactose, N-acetylgalactosamine, or N-acetylglucosamine. Like heparan ... There are two major families of carbohydrate sulfotransferases: heparan sulfotransferases and galactose/N-acetylgalactosamine/N ... which transfer sulfate to position 4 of non-reducing N-acetylgalactosamine (GalNAc) residues in both N-glycans and O-glycans. ... "Molecular cloning and characterization of a dermatan-specific N-acetylgalactosamine 4-O-sulfotransferase". J. Biol. Chem. 276 ( ...
... (EC 2.8.2.35, dermatan-specific N-acetylgalactosamine 4-O-sulfotransferase, dermatan-4- ... "Molecular cloning and characterization of a dermatan-specific N-acetylgalactosamine 4-O-sulfotransferase". The Journal of ... "Specificities of three distinct human chondroitin/dermatan N-acetylgalactosamine 4-O-sulfotransferases demonstrated using ... sulfotransferase-1, dermatan-4-sulfotransferase 1, D4ST-1, dermatan N-acetylgalactosamine 4-O-sulfotransferase, CHST14 protein ...
... (N-acetylgalactosamine-4-sulfatase, chondroitinsulfatase, chondroitinase, acetylgalactosamine 4-sulfatase, N- ... Galsulfase (N-acetylgalactosamine-4-sulfatase, recombinant human) was granted orphan drug designation by both the European ... N-acetylgalactosamine-4-sulfatase): potential role as a biomarker in prostate cancer". Prostate Cancer and Prostatic Diseases. ... This disease is caused by the lack of an enzyme called N-acetylgalactosamine 4-sulfatase, which is needed to break down ...
The sugars are usually a combination of N-acetylgalactosamine, D-glucose or D-galactose. A glycosphingolipid that has only one ...
Taniguchi N, Makita A (1984). "Purification and characterization of UDP-N-acetylgalactosamine: globotriaosylceramide beta-3-N- ... Identification of beta 3Gal-T3 as UDP-N-acetylgalactosamine:globotriaosylceramide beta 1,3-N-acetylgalactosaminyltransferase". ... Identification of four inactivating mutations in the UDP-N-acetylgalactosamine: globotriaosylceramide 3-beta-N- ... N-acetylgalactosamine). The beta3GalT genes are distantly related to the Drosophila Brainiac gene and have the protein coding ...
Taniguchi N, Makita A (1984). "Purification and characterization of UDP-N-acetylgalactosamine: globotriaosylceramide beta-3-N- ... Identification of beta 3Gal-T3 as UDP-N-acetylgalactosamine:globotriaosylceramide beta 1,3-N-acetylgalactosaminyltransferase". ...
Warren, G.; Tooze, J.; Tooze, S. A. (1988-05-01). "Site of addition of N-acetyl-galactosamine to the E1 glycoprotein of mouse ...
The first sugar is always N-acetyl-galactosamine (GalNAc), followed by other galactoses and sialic acid. In HSP and IgAN, these ...
The galactose component originates from UDP-galactose and the GalNAc component originates from UDP-N-acetylgalactosamine. These ... is an exopolysaccharide composed of galactose and N-acetylgalactosamine (GalNAc). It is commonly found in the biofilm and cell ...
UDP-N-acetylgalactosamine:polypeptide, N-acetylgalactosaminyltransferase, and UDP-N-acetylgalactosamine:protein N- ... UDP-N-acetylgalactosamine-glycoprotein, N-acetylgalactosaminyltransferase, UDP-N-acetylgalactosamine-protein N- ... polypeptide-N-acetylgalactosamine transferase, UDP-acetylgalactosamine-glycoprotein, acetylgalactosaminyltransferase, UDP- ... Takeuchi M, Yoshikawa M, Sasaki R, Chiba H (1985). "Purification and characterization of UDP-N-acetylgalactosamine-kappa-casein ...
The enzyme coded for by IA adds an N-acetylgalactosamine to a membrane-bound H antigen. The IB enzyme adds a galactose. The i ...
Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase Amado M, Almeida R, Schwientek T, Clausen H (December 1999). " ... Core 1 synthase, glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase, 1, also known as C1GALT1, is an enzyme which ...
"Site-Specific Incorporation of the Mucin-Type N-Acetylgalactosamine-α-O-threonine into Protein in Escherichia coli". Journal of ... "Site-specific incorporation of the mucin-type N-acetylgalactosamine-alpha-O-threonine into protein in Escherichia coli". ...
... characterization of a novel chondroitin sulfate glucuronyltransferase that transfers glucuronic acid to N-acetylgalactosamine ...
This family transfers an N-acetyl galactosamine to the hydroxyl group of a serine or threonine residue in the first step of O- ... "Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N- ...
Keratan sulfate N-Acetylgalactosamine (GalNAc) N-Acetyllactosamine synthase Wheat germ agglutinin, a plant lectin that binds to ... however this is much weaker than the inhibition seen with N-acetylgalactosamine (range 92-100%). It has been proposed as a ... "Inhibition of elastase enzyme release from human polymorphonuclear leukocytes by N-acetyl-galactosamine and N-acetyl- ...
2001). "Chromosomal localization and genomic organization for the galactose/ N-acetylgalactosamine/N-acetylglucosamine 6-O- ...
1998). "Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N- ...
"Functional conservation of subfamilies of putative UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferases in ...
N-Acetylgalactosamine (GalNAc), is an amino sugar derivative of galactose. In humans it is the terminal carbohydrate forming ... N-Acetylgalactosamine is necessary for intercellular communication, and is concentrated in sensory nerve structures of both ... Destruction of Blood Group A Activity by an Enzyme from Clostridium tertium Which Deacetylates N-Acetylgalactosamine in Intact ... Media related to N-Acetylgalactosamine at Wikimedia Commons. ... "Multivalent N-Acetylgalactosamine-Conjugated siRNA Localizes in ...
In enzymology, a N-acetylgalactosamine kinase (EC 2.7.1.157) is an enzyme that catalyzes the chemical reaction ATP + N-acetyl-D ... Other names in common use include GALK2, GK2, GalNAc kinase, and N-acetylgalactosamine (GalNAc)-1-phosphate kinase. Pastuszak I ... Thoden JB, Holden HM (2005). "The molecular architecture of human N-acetyl galactosamine kinase". J. Biol. Chem. 280 (38): ... Drake R, Elbein AD (1996). "Kidney N-acetylgalactosamine (GalNAc)-1-phosphate kinase, a new pathway of GalNAc activation". J. ...
... PubChem Notes: Acetylgalactosamine The N-acetyl derivative of galactosamine. ACETYLGALACTOSAMINE Galactose, 2-(acetylamino)-2-deoxy- N-[(3R,4R,5R,6R)-2,4,5-trihydroxy-6-(hydroxymethyl)oxan-3-yl]acetamide ...
The X-ray structure of the N-acetylgalactosamine deacetylase reveals the active site and mechanism of the founding member of an ... Crystal structure of an N-acetylgalactosamine deacetylase from F. plautii. *DOI: 10.2210/pdb6N1A/pdb ...
Uridine diphosphate-N-acetylgalactosamine , C17H27N3O17P2 , CID 1167 - structure, chemical names, physical and chemical ...
N Acetylgalactosamine 4 sulfate Sulfatase. An arylsulfatase that catalyzes the Hydrolysis of the 4-sulfate groups of the N- ...
Antibodies for proteins involved in N-acetylgalactosamine kinase activity pathways, according to their Panther/Gene Ontology ... Antibodies for proteins involved in N-acetylgalactosamine kinase activity pathways; according to their Panther/Gene Ontology ...
... we demonstrated production of an active recombinant human N-acetylgalactosamine-6-sulfatase (rhGALNS) enzyme in Escherichia ... Recombinant human N-acetylgalactosamine-6-sulfate sulfatase (GALNS) produced in the methylotrophic yeast Pichia pastoris. Sci ... Improvement in the production of the human recombinant enzyme N-acetylgalactosamine-6-sulfatase (rhGALNS) in Escherichia coli ... Characterization of a recombinant N-acetylgalactosamine-6-sulfate sulfatase produced in E. coli for enzyme replacement therapy ...
Mechanism of pH-dependent N-acetylgalactosamine binding by a functional mimic of the hepatocyte asialoglycoprotein receptor. ... N-ACETYLGALACTOSAMINE-SELECTIVE MUTANT OF MANNOSE-BINDING PROTEIN-A (QPDWG-HDRPY). *DOI: 10.2210/pdb1fif/pdb ...
A peptide mimetic of a ligand for the galactose/N-acetylgalactosamine-specific C-type lectin receptors (GCLR) exhibited ... Monocyte galactose/N-acetylgalactosamine-specific C-type lectin receptor stimulant immunotherapy of an experimental glioma. ... Monocyte galactose/N-acetylgalactosamine-specific C-type lectin receptor stimulant immunotherapy of an experimental glioma. ... Background: A peptide mimetic of a ligand for the galactose/N-acetylgalactosamine-specific C-type lectin receptors (GCLR) ...
Rabbit Polyclonal Anti-N-Acetylgalactosamine-6-Sulfatase/GALNS Antibody. Validated: WB, ICC/IF, IHC, IHC-P. Tested Reactivity: ... Additional N-Acetylgalactosamine-6-Sulfatase/GALNS Products. N-Acetylgalactosamine-6-Sulfatase/GALNS NBP1-32899 * N- ... Blogs on N-Acetylgalactosamine-6-Sulfatase/GALNS. There are no specific blogs for N-Acetylgalactosamine-6-Sulfatase/GALNS, but ... PTMs for N-Acetylgalactosamine-6-Sulfatase/GALNS Antibody (NBP1-32899). Learn more about PTMs related to N-Acetylgalactosamine- ...
View mouse Chst15 Chr7:132235780-132317228 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression
S. Ohtake-Niimi, S. Kondo, T. Ito et al., "Mice deficient in N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase are unable to ... S. Ohtake, Y. Ito, M. Fukuta, and O. Habuchi, "Human N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase cDNA is related to ... Chondroitin sulfate (CS) containing E-disaccharide units, glucuronic acid-N-acetylgalactosamine(4, 6-O-disulfate), at surfaces ... Expression of N-Acetylgalactosamine 4-Sulfate 6-O-Sulfotransferase Involved in Chondroitin Sulfate Synthesis Is Responsible for ...
This staining demonstrates glycoconjugate with terminal N-acetylgalactosamine (GalNAc) in periodic foci on the neuronal surface ... Postnatal appearance of glycoconjugate with terminal N-acetylgalactosamine on the surface of selected neurons in mouse brain ... This staining demonstrates glycoconjugate with terminal N-acetylgalactosamine (GalNAc) in periodic foci on the neuronal surface ...
Open-Label Study of Efficacy and Safety of Recombinant Human N-acetylgalactosamine 4-sulfatase in Patients With MPS VI. The ... Open-Label Study of Efficacy and Safety of Recombinant Human N-acetylgalactosamine 4-sulfatase in Patients With MPS VI. ... and pharmacokinetics of weekly intravenous infusions of 1 mg/kg recombinant human N-acetylgalactosamine 4-sulfatase (rhASB) in ...
... Lookup it up at Rhymes.net - the most comprehensive rhyming words ... Weve got 0 rhyming words for n-acetylgalactosamine-4-sulfatase ». What rhymes with n-acetylgalactosamine-4-sulfatase?. This ... Search for Song lyrics containing the word n-acetylgalactosamine-4-sulfatase. *Search for n-acetylgalactosamine-4-sulfatase on ... Know what rhymes with n-acetylgalactosamine-4-sulfatase? Have another rhyming word for n-acetylgalactosamine-4-sulfatase? Let ...
Poly(malic acid) bearing Doxorubicin and N-Acetyl Galactosamine as a site-specific prodrug for targeting hepatocellular ... Poly(malic acid) bearing Doxorubicin and N-Acetyl Galactosamine as a site-specific prodrug for targeting hepatocellular ... and/or N-Acetyl Galactosamine (NAcGal) for drug delivery. These poly(malic acid) derivatives were obtained by chemical ...
N-Acetylgalactosamine 6-Sulphatase. Principle Of Method: Two methods are available for this assay, both in use in the ... The enzyme releases sulphate from galactose 6-sulphate residues in keratan sulphate and from N-acetylgalactosamine 6-sulphate ...
Plasma and Liver Protein Binding of N-Acetylgalactosamine-Conjugated Small Interfering RNA. Sara C. Humphreys, Mai B. Thayer, ... Plasma and Liver Protein Binding of N-Acetylgalactosamine-Conjugated Small Interfering RNA ...
Core 1 synthase, glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase, 1. T-synthase, C1GALT1, beta 1,3- ... glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase, 1(T-synthase) ...
Isolation and partial characterization of an N-acetylgalactosamine-specific lectin from winter-aconite (Eranthis hyemalis) root ... Isolation and partial characterization of an N-acetylgalactosamine-specific lectin from winter-aconite (Eranthis hyemalis) root ... Isolation and partial characterization of an N-acetylgalactosamine-specific lectin from winter-aconite (Eranthis hyemalis) root ... Hapten inhibition assays indicated that the winter-aconite lectin is specific for N-acetylgalactosamine. In addition, the ...
CHST15; carbohydrate (N-acetylgalactosamine 4-sulfate 6-O) sulfotransferase 15; carbohydrate sulfotransferase 15; B cell RAG ... associated protein; BRAG; GALNAC4S 6ST; KIAA0598; N acetylgalactosamine 4 sulfate 6 O sulfotransferase; hBRAG; B-cell RAG- ...
N-Acetylgalactosamine-4-sulfotransferase-1 (GalNAc-4-ST1, CHST8) and N-Acetylgalactosamine-4-sulfotransferase-2 (GalNAc-4-ST2, ... Baenziger J.U. (2014) N-Acetylgalactosamine-4-sulfotransferase-1 (GalNAc-4-ST1, CHST8) and N-Acetylgalactosamine-4- ... Kang HG, Evers MR, Xia G, Baenziger JU, Schachner M (2001) Molecular cloning and expression of an N-acetylgalactosamine-4-O- ... Okuda T, Sawada T, Nakano H, Matsubara K, Matsuda Y, Fukuta M, Habuchi O (2003) Mouse N-acetylgalactosamine 4-sulfotransferases ...
N-acetylgalactosamine (GalNAc) transfer to the common carbohydrate-protein linkage region of sulfated glycosaminoglycans: ... a novel N-acetylgalactosamine(GalNAc) transferase was discovered in fetalbovine serum. The enzyme catalyzed the transfer of[3H] ...
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... converting UDP-N-acetylglucosamine into UDP-N-acetylgalactosamine, is responsible for the presence of N-acetylgalactosamine in ... Both strains produced the same EPS composed of galactose, glucose, and N-acetylgalactosamine. Further, it was demonstrated that ... UDP-N-Acetylglucosamine 4-Epimerase Activity Indicates the Presence of N-Acetylgalactosamine in Exopolysaccharides of ... UDP-N-Acetylglucosamine 4-Epimerase Activity Indicates the Presence of N-Acetylgalactosamine in Exopolysaccharides of ...
UDP-N-acetylgalactosamine ligand page. Quantitative data and detailed annnotation of the targets of licensed and experimental ... Molecular characterization of human UDP-glucuronic acid/UDP-N-acetylgalactosamine transporter, a novel nucleotide sugar ...
Molecular structure of the "low molecular weight antigen" of Toxoplasma gondii: A glucose α1-4 N-acetylgalactosamine makes free ... Molecular structure of the "low molecular weight antigen" of Toxoplasma gondii: A glucose α1-4 N-acetylgalactosamine makes free ...
Gleich, Otto (1994) The distribution of N-acetylgalactosamine in the cochlear nucleus of the gerbil revealed by lectin binding ... The distribution of N-acetylgalactosamine in the cochlear nucleus of the gerbil revealed by lectin binding with soybean ... Gerbil; Brain stem; Cochlear nucleus; Lectin; N-acetylgalactosamine; Glycoconjugate References. Dewey-Dezimal-Klassifikation:. ... was used to characterise the distribution of N-acetylgalactosamine in the cochlear nucleus of the mongolian gerbil. SBA bound ...
Glen Report 29.14: N-acetylgalactosamine (GalNAc) Oligonucleotide Conjugates * Glen Report 29.15: Sequence Modification using ... Glen Report 29.14: N-acetylgalactosamine (GalNAc) Oligonucleotide Conjugates. Oligonucleotides are predominantly hydrophilic ... therapeutic delivery as evidenced by the work of Alnylam Pharmaceuticals which has developed multivalent N-acetylgalactosamine ...
  • N-Acetylgalactosamine (GalNAc), is an amino sugar derivative of galactose. (wikipedia.org)
  • Other names in common use include GALK2, GK2, GalNAc kinase, and N-acetylgalactosamine (GalNAc)-1-phosphate kinase. (wikipedia.org)
  • This staining demonstrates glycoconjugate with terminal N-acetylgalactosamine (GalNAc) in periodic foci on the neuronal surface. (nih.gov)
  • During the course of a study to elucidate the role ofmodification of the common polysaccharide-protein linkagestructure, GlcAb1-3Galb1-3Galb1-4Xylb1-O-Ser, inbiosynthetic sorting mechanisms of the different sulfatedglycosaminoglycan chains, a novel N-acetylgalactosamine(GalNAc) transferase was discovered in fetalbovine serum. (diva-portal.org)
  • To characterize potential differences in recognition of terminal N-acetylgalactosamine (GalNAc) on IgA1, we evaluated the binding characteristics of several commercial preparations of GalNAc-specific lectins using a panel of IgA1 and, as controls, IgA2 and IgG myeloma proteins. (forskningsdatabasen.dk)
  • In the biosynthetic pathway that forms the sialyl-Tn (STn) antigen, a family of polypeptide N -acetylgalactosamine (GalNAc)-transferases (ppGalNAcT) initially adds a GalNAc residue to Ser or Thr of the peptide. (nih.gov)
  • CLEC4F, a member of C-type lectin, was first purified from rat liver extract with high binding affinity to fucose, galactose (Gal), N-acetylgalactosamine (GalNAc), and un-sialylated glucosphingolipids with GalNAc or Gal terminus. (nih.gov)
  • It is localized to the golgi membrane, and catalyzes the transfer of sulfate to the C4 hydroxyl of beta-1,4-linked N-acetylgalactosamine (GalNAc) flanked by glucuronic acid residue in chondroitin. (nih.gov)
  • Transfers N-acetylgalactosamine (GalNAc) from UDP-GalNAc to N-acetylglucosamine-beta-benzyl with a beta-1,4-linkage to form N,N'-diacetyllactosediamine, GalNAc-beta-1,4-GlcNAc structures in N-linked glycans and probably O-linked glycans. (genecards.org)
  • B4GALNT3 transfers N-acetylgalactosamine (GalNAc) onto glucosyl residues to form N,N-prime-diacetyllactosediamine (LacdiNAc, or LDN), a unique terminal structure of cell surface N-glycans (Ikehara et al. (genecards.org)
  • Catalyzes the transfer of sulfate to position 4 of non-reducing N-acetylgalactosamine (GalNAc) residues in both N-glycans and O-glycans. (uniprot.org)
  • Carbohydrate sulphotransferases 8 and 9, which transfer sulphate to position 4 of non-reducing N-acetylgalactosamine (GalNAc) residues in both N-glycans and O-glycans [ PMID: 11445554 ]. (ebi.ac.uk)
  • Molecular cloning and expression of two distinct human N-acetylgalactosamine 4-O-sulfotransferases that transfer sulfate to GalNAc beta 1-->4GlcNAc beta 1-->R in both N- and O-glycans. (ebi.ac.uk)
  • Monocyte galactose/N-acetylgalactosamine-specific C-type lectin receptor stimulant immunotherapy of an experimental glioma. (dovepress.com)
  • A peptide mimetic of a ligand for the galactose/N-acetylgalactosamine-specific C-type lectin receptors (GCLR) exhibited monocyte-stimulating activity, but did not extend survival when applied alone against a syngeneic murine malignant glioma. (dovepress.com)
  • Both strains produced the same EPS composed of galactose, glucose, and N-acetylgalactosamine. (hud.ac.uk)
  • A Golgi vesicle enriched fraction of Saccharomyces cerevisiae expressing SQV-7 transported UDP-glucuronic acid, UDP-N-acetylgalactosamine, and UDP-galactose (Gal) in a temperature-dependent and saturable manner. (elsevier.com)
  • In the ABO system, type A RBCs are distinguished by an amino sugar (alpha-1,3-linked- N -acetylgalactosamine) antigen, whereas type B antigen has a sugar (galactose). (medscape.com)
  • Previously, we demonstrated production of an active recombinant human N-acetylgalactosamine-6-sulfatase (rhGALNS) enzyme in Escherichia coli as a potential therapeutic alternative for mucopolysaccharidosis IVA. (nature.com)
  • Western Blot: N-Acetylgalactosamine-6-Sulfatase/GALNS Antibody [NBP1-32899] - Sample (30 ug of whole cell lysate) A: H1299 7.5% SDS PAGE diluted at 1:1000. (novusbio.com)
  • Immunocytochemistry/ Immunofluorescence: N-Acetylgalactosamine-6-Sulfatase/GALNS Antibody [NBP1-32899] - Paraformaldehyde-fixed HeLa, using GALNS antibody (Green) at 1:500 dilution. (novusbio.com)
  • Immunohistochemistry-Paraffin: N-Acetylgalactosamine-6-Sulfatase/GALNS Antibody [NBP1-32899] - Paraffin-embedded NCI-N87 xenograft, using antibody at 1:100 dilution. (novusbio.com)
  • This gene encodes N-acetylgalactosamine-6-sulfatase which is a lysosomal exohydrolase required for the degradation of the glycosaminoglycans, keratan sulfate, and chondroitin 6-sulfate. (novusbio.com)
  • What rhymes with n-acetylgalactosamine-4-sulfatase? (rhymes.net)
  • This page is about the various possible words that rhymes or sounds like n-acetylgalactosamine-4-sulfatase . (rhymes.net)
  • We couldn't find any rhymes for the word n-acetylgalactosamine-4-sulfatase . (rhymes.net)
  • A graphical representation of the words that rhyme with n-acetylgalactosamine-4-sulfatase . (rhymes.net)
  • Have another rhyming word for n-acetylgalactosamine-4-sulfatase ? (rhymes.net)
  • Is n-acetylgalactosamine-4-sulfatase wrong or has spelling mistakes? (rhymes.net)
  • Morquio A is an autosomal recessive mucopolysaccharidosis caused by reduced or absent N-acetylgalactosamine-6-sulfate sulfatase (GALNS) enzyme activity. (mayocliniclabs.com)
  • Maroteaux-Lamy syndrome, or mucopolysaccharidosis type VI (MPS-VI), is a lysosomal storage disorder characterized by the defective degradation of dermatan sulfate due to the deficiency of N-acetylgalactosamine-4-sulfatase (4S). (edu.au)
  • Mucopolysaccharidosis type VI: Structural and clinical implications of mutations in N-acetylgalactosamine-4-sulfatase. (medlineplus.gov)
  • Purification and properties of human N-acetylgalactosamine-6-sulfate sulfatase. (genome.jp)
  • In enzymology, a N-acetylgalactosamine kinase (EC 2.7.1.157) is an enzyme that catalyzes the chemical reaction ATP + N-acetyl-D-galactosamine ⇌ {\displaystyle \rightleftharpoons } ADP + N-acetyl-alpha-D-galactosamine 1-phosphate Thus, the two substrates of this enzyme are ATP and N-acetyl-D-galactosamine, whereas its two products are ADP and N-acetyl-alpha-D-galactosamine 1-phosphate. (wikipedia.org)
  • The molecular architecture of human N-acetylgalactosamine kinase. (medlineplus.gov)
  • Further, it was demonstrated that the activity of the precursor-producing enzyme UDP-N-acetylglucosamine 4-epimerase, converting UDP-N-acetylglucosamine into UDP-N-acetylgalactosamine, is responsible for the presence of N-acetylgalactosamine in the EPS repeating units of both strains. (hud.ac.uk)
  • UDP-N-Acetylgalactosamine can be used for glycosylation of target molecules with a suitable enzyme. (roche.com)
  • Background: We investigated the activation of N-acetylgalactosamine-transferase11 (GALNT11) and the role of cyclophosphamide and cytarabine in expression of this enzyme in AML and CML patients. (ac.ir)
  • A single mutation in a gene that codes for UDP N -acetylgalactosamine 4-epimerase ( gne ) renders a strain with the O − phenotype (LPS without O-antigen molecules) in serotype O34 ( 9 ). (asm.org)
  • Chondroitin sulfate (CS) containing E-disaccharide units, glucuronic acid- N -acetylgalactosamine(4, 6- O -disulfate), at surfaces of tumor cells plays a key role in tumor metastasis. (hindawi.com)
  • Chondroitin 6-sulphotransferase catalyses the transfer of sulphate to position 6 of the N-acetylgalactosamine residue of chondroitin [ PMID: 18697746 ]. (ebi.ac.uk)
  • In this study, to clarify the role of E-units in the metastasis and to search for potential molecular targets for anticancer drugs, the isolation and characterization of Lewis lung carcinoma (LLC) cells stably downregulated by the knockdown for the gene encoding N -acetylgalactosamine 4- O -sulfate 6- O -sulfotransferase (GalNAc4S-6ST), which is responsible for the formation of E-units in CS chains, were performed. (hindawi.com)
  • Molecular characterization of human UDP-glucuronic acid/UDP-N-acetylgalactosamine transporter, a novel nucleotide sugar transporter with dual substrate specificity. (guidetopharmacology.org)
  • Molecular cloning and characterization of a dermatan-specific N-acetylgalactosamine 4-O-sulfotransferase. (ebi.ac.uk)
  • Acetylgalactosamine The N-acetyl derivative of galactosamine. (scitoys.com)
  • UDP-N-Acetylgalactosamine is an activated sugar, and can be used for in vitro glycoengineering of glycoproteins, e.g . therapeutic proteins. (roche.com)
  • Identification of N-Acetylgalactosamine-containing glycoproteins PEB3 and CgpA in Campylobacter jejuni. (kingston.ac.uk)
  • Linton, D. , Allan, E. , Karlyshev, A.V. and Wren, B.W. (2001) Identification of N-Acetylgalactosamine-containing glycoproteins PEB3 and CgpA in Campylobacter jejuni. (kingston.ac.uk)
  • The results are discussed with respect to findings in other brain areas and the possible co-localisation of gamma aminobutyric acid (GABA), parvalbumin and N-acetylgalactosamine. (uni-regensburg.de)
  • The binding sites of Sodium atom in the structure of CPGH89CBM32-5, From Clostridium Perfringens, in Complex With N-Acetylgalactosamine (pdb code 4aax ). (atomistry.com)
  • N-Acetylgalactosamine is necessary for intercellular communication, and is concentrated in sensory nerve structures of both humans and animals. (wikipedia.org)
  • The X-ray structure of the N-acetylgalactosamine deacetylase reveals the active site and mechanism of the founding member of an esterase family. (rcsb.org)
  • EC 2.4.1.41) family, which initiate O-linked glycosylation of mucins (see MUC3A, MIM 158371) by the initial transfer of N-acetylgalactosamine (GalNAc) with an alpha-linkage to a serine or threonine residue. (utsouthwestern.edu)
  • CHST8 (carbohydrate (N-acetylgalactosamine 4-0) sul. (lovd.nl)
  • In their work on zebrafish, Baskin, Bertozzi and their colleagues soaked zebrafish embryos in the artificial sugar N-azidoacetylgalactosamine, which the embryo cells then used as a carbohydrate building block to replace the natural sugar N-acetylgalactosamine. (blogspot.com)
  • This modification leaves the A-specific sugar as galactosamine (N-acetylgalactosamine with the acetyl group removed = galactosamine). (labmedicineblog.com)