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(13) NMR spectra of chitin oligomers in aqueous solution were analyzed for a reference of assignment of solid state (13)C NMR spectra of chitin and N-acyl chitosans, and also of (13)C chemical shift data in aqueous solution.

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Non-catalytic synthesis of 2-acetamido-2,3-dideoxy-d-erythro-hex-2- enofuranose (Chromogen I) and 3-acetamido-5-(1?,2?-dihydroxyethyl) furan (Chromogen III) from N-acetyl-d-glucosamine (GlcNAc) was achieved, with the highest yields of 23.0% and 23.1%, respectively, in high-temperature water at 120-220 C and 25 MPa with a reaction time of 7-39 s.

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UDP-6-Deoxy-D-galactose and UDP-6-deoxy-6-fluoro-D-galactose were synthesized and their transfer to 2-acetamido-2-deoxy-D-glucose (N-acetyl-D-glucosamine) by beta-(1 ? 4)-galactosyltransferase was examined. The transfer rates of 6-deoxy-D-galactose and 6-deoxy-6-fluoro-D-galactose were 1.3 and 0.2% of that of D-galactosyl transfer, respectively. The 2-acetamido-4-O-(6-deoxy-beta-D-galactopyranosyl)-2-deoxy-D-glucopyranos e (6′-deoxy-N-acetyllactosamine) and methyl 2-acetamido-4-O-(6-deoxy-6-fluoro-beta-D-galactopyranosyl)-2-deoxy-D-glu copyranoside (6′-deoxy-6′-fluoro-N-acetyllactosamine) were synthesized enzymatically in 30 and 59% yields, respectively. Further, 6-deoxy-D-galactose could be completely transferred to N-linked type biantennary oligosaccharides having two N-acetyl-D-glucosaminyl residues at the nonreducing end to give the corresponding penta- and hepta-saccharides in 55 and 57% yields, respectively. An assay of 6-deoxy-D-galactosyl transfer using asialo agalacto alpha1-acid glycoprotein as an acceptor suggested that 6-deoxy-D-galactose was transferred to about 30% of the N-acetyl-D-glucosaminyl residues in the N-linked oligosaccharides of the glycoprotein.

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Tetrahydropyran – Wikipedia,
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The reactions of sodium benzoate with a series of trimesylates derived from glucosamine have been examined in an attempt to gain facile access to galactosamine analogues. Trimesylate 17, in which the amino group was protected as a phthalimide, underwent double displacement at positions 4 and 6 to give the dibenzoate 18 with the desired galactosamine configuration. In contrast, trimesylates 21 and 27, in which the amino groups were protected as acetamides, unexpectedly underwent double displacement at positions 3 and 6, giving products 22 and 28, respectively, with allosamine configurations.

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L-Rhamnose-binding lectins were isolated from white-spotted charr (Salvelinus leucomaenis) eggs to understand the distribution and molecular evolution of the lectins in Salmonidae. Only two L-rhamnose-binding lectins, named WCL1 and WCL3, were isolated from white-spotted charr eggs, though three lectins, named STL1, STL2, and STL3, had been obtained from steelhead trout (Oncorhynchus mykiss) eggs. The cDNAs of WCL1 and WCL3 included 1,245 and 838 bp nucleotides with open reading frames of 933 and 651 nucleotides, respectively, and encoded for the complete amino acid sequences of mature proteins consisted of 288 (WCL1) and 195 (WCL3) residues, and signal sequences of 23 and 22 residues, respectively. WCLs were composed of three (for WCL1) or two (for WCL3) tandemly repeated homologous domains, which consisted of about 95 amino acid residues, and showed 91 and 93% sequence identities to STL1 and STL3, respectively. The mRNAs of WCL1 and WCL3 were detected exclusively in liver and ovary, respectively, however, neither a protein nor mRNA corresponding to STL2 could be identified in white-spotted charr. The phylogenetic tree of the sequences encoding carbohydrate recognition domains of 7 lectins from 4 species shows 5 functional clusters and their evolutional process. These results indicate that multiple L-rhamnose-binding isolectins have diverged by gene duplication and exon shuffling to play various biological roles in each species.

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Six for the price of one: From a single precursor, dehydroalanine, six distinct post-translational modifications can be site-selectively installed on histone proteins (see figure), including the first site-selective phosphorylation and glycosylation of histones. Direct observation of histone deacetylase activity on a full-length modified histone as well as its interactions with both chromatin reader and writer/eraser proteins are reported.

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Tetrahydropyran – Wikipedia,
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GalNAc (1) was straightforwardly prepared from GlcNAc (2a) in six steps. Selective protection of the hydroxy groups on the C-1, C-3, and C-6 positions at the same time was performed by the treatment of TBDPS chloride (5.5 eq.) in DMF in 70% yield. The nucleophilic attack with CsOAc or KOBz on the chloromethylsulfonyloxy group at C-4 worked well (69-77% yield), accompanied by an unexpected rearrangement, to give the furanose products (6). The deprotection of all silyl and acyl groups under acidic conditions and the re-acetylation provided GalNAc (1) in 51% yield.

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Recommanded Product: N-((2S,3R,4R,5R,6R)-2,4,5-Trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-3-yl)acetamide, As an important bridge between the micro and macro material world, chemistry is one of the main methods and means for humans to understand and transform the material world. 14215-68-0, Name is N-((2S,3R,4R,5R,6R)-2,4,5-Trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-3-yl)acetamide, molecular formula is C8H15NO6. In a Article,once mentioned of 14215-68-0

N-acetyl-D-glucosamine (GlcNAc) is a monosaccharide that polymerizes linearly through (1,4)-beta-linkages. GlcNAc is the monomeric unit of the polymer chitin. GlcNAc is a basic component of hyaluronic acid and keratin sulfate found on the cell surface. The aim of this study was to examine amino acid metabolism after oral GlcNAc administration in dogs. Results showed that plasma levels of ectoine were significantly higher after oral administration of GlcNAc than prior to administration (p < 0.001). To our knowledge, there have been no reports of increased ectoine concentrations in the plasma. The mechanism by which GlcNAc administration leads to increased ectoine plasma concentration remains unclear; future studies are required to clarify this mechanism. Note that a catalyst decreases the activation energy for both the forward and the reverse reactions and hence accelerates both the forward and the reverse reactions.Recommanded Product: N-((2S,3R,4R,5R,6R)-2,4,5-Trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-3-yl)acetamide, you can also check out more blogs about14215-68-0

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Tetrahydropyran – Wikipedia,
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Beta-N-Acetylhexosaminidases (EC 3.2.1.52, belonging to CAZy GH families 3, 20 and 84) have recently gained a lot of attention, not only due to their implication in human physiology and disease, but also due to their great potential in the enzymatic synthesis of carbohydrates and glycomimetics. GH family 20 Beta-N-acetylhexosaminidases, and GH family 3 and 84 beta-N-acetylglucosaminidases from all kinds of organisms have been intensively studied from the point of view of their physiological roles, reaction mechanisms, structure and inhibition. Thanks to their outstanding substrate promiscuity, extracellular Beta-N-acetylhexosaminidases from filamentous fungi are able to cleave and transfer substrates bearing various functionalities, ranging from carboxylates, sulfates, acylations to azides, and even 4-deoxy glycosides. Thus, they have proved to be versatile biosynthetic tools for the preparation of both natural and modified hexosaminides under mild conditions with good yields.

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The application of N-glycosyl-N-alkyl-methoxyamine bi-functional linkers for the synthesis of a variety of glycoconjugates is described. The linker contains a specific functional group, such as an amine, azide, thiol, or carboxylic acid, which can be used for conjugation methodologies that include amide ligation, sulfonylation, copper-mediated Huisgen cycloaddition or thiol-maleimide coupling. In this way, glycoconjugates equipped with biotin, a fluorescent reporter, or a protein were efficiently synthesised, thus demonstrating the versatility of this type of oxyamine linker for the construction of glycoconjugate probes.

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