Results 241 to 250 of about 14,921,471 (288)

Biomimetic nanochannels platform for detecting N-acetylglucosamine analogues

, 2020
N-acetylglucosamine analogues exist in nature as an important saccharide in human body and can regulate a variety of life activities captured through biological nanochannels.
Yue Sun, Shirong Cheng, Junkai Ma, Fei Zhu, W. Hong, Haibing Li   +5 more
semanticscholar   +1 more source

Conversion of N-Acetylglucosamine to Protected Amino Acid over Ru/C Catalyst

ACS Sustainable Chemistry and Engineering, 2018
Chitin is the most abundant marine biomass, containing nitrogen atoms in its monomer units, N-acetylglucosamine (NAG). Thus, NAG is a potential feedstock for the production of renewable organonitrogen chemicals.
Kota Techikawara, Hirokazu Kobayashi, A. Fukuoka   +2 more
semanticscholar   +1 more source

UDP-N-acetylglucosamine: Lysosomal enzyme N-acetylglucosamine-1-phosphotransferase

1984
Publisher Summary UDP-N-acetylglucosamine: lysosomal enzyme, N-acetylglucosamine-1-phosphotransferase (N-acetylglucosaminylphosphotransferase), transfers N-acetylglucosamine 1-phosphate en bloc to the C-6 oxygen of certain mannose residues in high mannose-type oligosaccharides of lysosomal enzymes.
M L, Reitman, L, Lang, S, Kornfeld
openaire   +2 more sources

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
openaire   +2 more sources

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
openaire   +1 more source

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
openaire   +2 more sources

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
openaire   +2 more sources

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
openaire   +2 more sources

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
openaire   +2 more sources

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 ...
openaire   +2 more sources