N-acetylglucosamine


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N-a·ce·tyl·glu·co·sam·ine

(a-sĕ'til-glū-cōs'a-mēn),
An acetylated amino sugar that is an important moiety of glycoproteins.
Farlex Partner Medical Dictionary © Farlex 2012
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Finally, UDP-N-acetylglucosamine selectivity is governed by extensive hydrogen-bonding as well as the stereospecific architecture of the N-acetylglucosamine binding pocket that would interfere with the binding of a sugar with axial substituents (Figure 3) [26].
Korekane et al., "Hypoxic regulation of glycosylation via the N-acetylglucosamine cycle," Journal of Clinical Biochemistry and Nutrition, vol.
This is the first study aiming to carry out biochemical and histopathological assessments of possible hepatic-oxidative stress induced by paracetamol and phenacetin, when used in therapeutic doses, in male albino rats and also to compare and detect which of the three antioxidants (N-acetylcysteine, N-acetylmethionine, and N-acetylglucosamine) has the best antioxidant and hepatoprotective efficacy against the drug-induced liver injury, if any.
(A) Intron 20 of O-linked N-acetylglucosamine transferase (OGT) from European and Chinese pig breeds.
The retention times of N-acetylated chitohexaoses increase with the decreasing of N-acetylglucosamine unit numbers.
They catalyze the hydrolysis of the b-1, 4-linkages between N-acetylglucosamine residues of chitin.
Lysozyme could hydrolyze the bindings between Nacetylmuramic acid and N-acetylglucosamine in some bacterial cell wall.
Chemically, it is a natural polymer of N-acetylglucosamine, a relative of glucose and cellulose.
A standard sample of 0.01 mol/L N-acetylglucosamine was prepared with NMR diluent.
PIA biosynthesis is carried out by the proteins encoded by the ica gene operon: N-acetylglucosamine transferase (icaA and icaD), PIA deacylase (icaB), PIA exporter (icaC) and the regulatory gene (icaR) [12 13].
Abstract Chitin is a naturally occurring insoluble linear AY1-4 linked polymer of N-acetylglucosamine and a common constituent of the fungal cell wall and exoskeleton of arthropods.
Numerous proteins, including kinases and phosphatases, have been identified as targets of O-GlcNAc modification--that is, the O-linked attachment of N-acetylglucosamine (O-GlcNAc) to serine and threonine residues of nuclear and cytoplasmic proteins (10-12).

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