Results 171 to 180 of about 60,876 (204)

Role of acetylglucosamine in chitin synthesis in crayfish—II. Enzymes in the epidermis for incorporation of acetylglucosamine into UDP-acetylglucosamine

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1973
Abstract 1. 1. Activity of an enzyme which phosphorylates acetyglucosamine has been found in the epidermis of crayfish. This activity does not appear to be competitively inhibited by glucose. 2. 2. A quantitative assay based on area of epidermis was developed for UDP-acetylglucosamine pyrophosphorylase.
J F, Gwinn, J R, Stevenson
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TERMINAL N-ACETYLGLUCOSAMINE IN CHRONIC SYNOVITIS

Rheumatology, 1990
The distribution of terminal GlcNAc residues in normal and diseased synovial tissue has been studied using a mouse monoclonal antibody (mAb) which binds to terminal N-acetylglucosamine (GlcNAc). Normal human connective tissue, including synovium, showed no staining for terminal GlcNAc.
M, Sharif, G, Rook, L S, Wilkinson, J G, Worrall, J C, Edwards   +4 more
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N-acetylglucosamine-6-O-sulfotransferases

2002
N-acetylglucosamine-6-O-sulfotransferase (GlcNAc6ST) transfers a sulfate group from PAPS to an N-acetylglucosamine residue, which is usually located at the non-reducing end of glycoconjugates. It is important to note that sulfation proceeds the elongation of the glycan chain.
Kenji Uchimura, Takashi Muramatsu
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Sequence of cloned enzyme IIN-acetylglucosamine of the phosphoenolpyruvate:N-acetylglucosamine phosphotransferase system of Escherichia coli

Biochemistry, 1988
In Escherichia coli, N-acetylglucosamine (nag) metabolism is joined to glycolysis via three specific enzymes that are the products of the nag operon. The three genes of the operon, nagA, nagB, and nagE, were found to be carried by a colicin plasmid, pLC5-21, from a genomic library of E. coli [Clarke, L., & Carbon, J. (1976) Cell (Cambridge, Mass.) 9,91-
K G, Peri, E B, Waygood
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Intestinal absorption of glucosamine and N-acetylglucosamine

Experientia, 1972
E stato studiato l'assorbimento della glucosamina e della N-acetilglucosamina utilizzando segmenti intestinali tagliati trasversalmente (strips) e sacchetti di intestino tenue di ratto. Il flusso di trasporto della glucosamina nelle cellule intestinali e mediato da carrier, indipendente dallo Na+ e procede senza accumulo attivo.
G, Tesoriere, F, Dones, D, Magistro, L, Castagnetta   +3 more
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The preparation of UDP-N-acetylgalactosamine from UDP-N-acetylglucosamine employing UDP-N-acetylglucosamine-4-epimerase

Analytical Biochemistry, 1982
Abstract A rapid, simple, and inexpensive method has been developed for preparing UDP- N -acetylgalactosamine in amounts sufficient for several thousand assays of enzymes that employ this nucleotide sugar as substrate. The UDP- N -acetylglucosamine-4-epimerase in extracts of porcine submaxillary glands was used to convert UDP- N -acetylglucosamine to
F, Piller, A E, Eckhardt, R L, Hill
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Regulation of n-acetylglucosamine uptake in yeast

Biochimica et Biophysica Acta (BBA) - Biomembranes, 1979
Various yeasts have been investigated for their ability to grow on N-acetylglucosamine as the sole carbon source and only those which are associated with the disease, candidiasis, gave positive results. The yeasts unable to grow on N-acetylglucosamine lacked the capacity to transport the aminosugar across the cell membrane.
B, Singh, A, Datta
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Binding of N-acetylglucosamine tetrasaccharide to lysozyme

Archives of Biochemistry and Biophysics, 1973
The β(1→4)-linked tetrasaccharide derived from N -acetylglucosamine binds to lysozyme differently than the trimer. The apparent enthalpy of binding of the tetramer is 2.8 kcal/mole less negative than that of the trimer. Because of enthalpy-entropy compensation, the free energy of binding of tetramer and trimer differ only slightly (by 0.3 kcal at 25°C)
S K, Banerjee, J A, Rupley
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Synapsins Contain O‐Linked N‐Acetylglucosamine

Journal of Neurochemistry, 1991
Abstract: The neuron‐specific synaptic vesicle‐associated phosphoproteins synapsin I and synapsin II were shown to contain terminal 7V‐acetylglucosamine (GlcNAc) residues as determined by specific labeling with bovine galactosyltrans‐ferase and UDP‐[3H]galactose.
T, Lüthi, R S, Haltiwanger, P, Greengard, M, Bähler   +3 more
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Glycan‐dependent signaling: O‐linked N‐acetylglucosamine

The FASEB Journal, 2001
The addition of O‐linked N‐acetylglucosamine (O‐GlcNAc) to target proteins may serve as a signaling modification analogous to protein phosphor‐ylation. Like phosphorylation, O‐GlcNAc is a dynamic modification occurring in the nucleus and cytoplasm. Various analytical methods have been developed to detect O‐GlcNAc and distinguish it from glycosylation ...
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