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De Novo Biosynthesis of Difucosyllactose by Artificial Pathway Construction and α1,3/4-Fucosyltransferase Rational Design in Escherichia coli.

Journal of Agricultural and Food Chemistry
Difucosyllactose (DFL) is a significant and plentiful oligosaccharide found in human breast milk. In this study, an artificial metabolic pathway of DFL was designed, focusing on the de novo biosynthesis of GDP-fucose from only glycerol. This was achieved
Yingying Zhu   +8 more
semanticscholar   +1 more source

Characterization of fucosyltransferase activity during mouse spermatogenesis: evidence for a cell surface fucosyltransferase

Biochemistry, 1989
Fucosyltransferase activity was quantified in mouse germ cells at different stages of spermatogenesis. Specifically, fucosyltransferase activities of pachytene spermatocytes, round spermatids, and cauda epididymal sperm were compared. Fucosyltransferase activity of mixed germ cells displayed an apparent Vmax of 17 pmol (mg of protein)-1 min-1 and an ...
D.R. Armant   +2 more
openaire   +3 more sources

Fucosyltransferase (α1,2/ α1,3/ α1,4-fucosyltransferases)

2009
Many studies using monoclonal antibodies have demonstrated that fucosylated carbohydrate chains are involved in various physiological functions including development, neuronal activity, and cancerous transformation. The genes encoding fucosyltransferases which synthesize fucosylated carbohydrate antigens have been cloned, and their function has been ...
Takashi Kudo, Hisashi Narimatsu
openaire   +2 more sources

Cloning of a rat alpha1,3-fucosyltransferase gene: a member of the fucosyltransferase IV family.

Glycoconjugate journal, 1997
We report the cloning of a rat alpha1,3-fucosyltransferase gene (rFuc-T), isolated from a rat genomic library by a PCR-cross-hybridization based cloning approach using primers derived from the conserved region of human alpha1,3-Fuc-T sequences. Comparison of the rFuc-T predicted amino acid sequence with those of previously cloned human and murine ...
Robert H. McCluer   +3 more
openaire   +3 more sources

Occurrence and specificities of α3-fucosyltransferases

The Histochemical Journal, 1992
The Le(x) (CD15) carbohydrate antigen and sialylated and oligomeric derivatives thereof have been implicated in cell adhesion processes. Expression of these antigens is developmentally regulated and (re)occurrence of several members of this group has been reported in malignant transformation of cells.
T.J. de Vries, D. H. Van Den Eijnden
openaire   +2 more sources

Production of 3-Fucosyllactose in Engineered Escherichia coli with α-1,3-Fucosyltransferase from Helicobacter pylori.

Biotechnology Journal, 2019
3-Fucosyllactose (3-FL), one of the major oligosaccharides in human breast milk, is produced in engineered Escherichia coli. In order to search for a good α-1,3-fucosyltransferase, three bacterial α-1,3-fucosyltransferases are expressed in engineered E ...
Sang-Min Jung   +2 more
semanticscholar   +1 more source

Study of the Fucosyltransferase System in Intestinal Microsomes

Enzyme, 1988
Fucosyltransferase activity of rat small intestine microsomes is solubilized by 0.5% Triton X-100. The solubilized activity can be purified up to 8,300-fold using DEAE-cellulose and affinity chromatography on GDP-Sepharose. At this step, chromatography on Sephadex G15 separates different specificities: N-acetylglucosaminide-alpha-(1,3 ...
Richard M   +4 more
openaire   +3 more sources

Daily variation of rat brain fucosyltransferase

Biochemical and Biophysical Research Communications, 1981
Abstract Glycoprotein fucosyltransferase activity was investigated in rat brain during 24 h periods. Up to 50 % variations were detected without correlations with either lights on or off, while acetylcholinesterase located in same membrane fractions showed no level variations.
Pierre Louisot, P. Broquet, Monique Leon
openaire   +3 more sources

α6-Fucosyltransferase (FUT8)

2002
GDP-L-FucN-acetyl-β-D-glucosaminide α1-6fucosyltransferase (FUT8) catalyzes the transfer of fucose from GDP-Fuc to N-linked-type complex glycoproteins, as shown in Fig. 1. The enzymatic products, α1,6-fucosylated (core fucosylated) N-glycans, are commonly observed in many glycoproteins, and are especially abundant in brain tissue. It is well known that
Eiji Miyoshi, Naoyuki Taniguchi
openaire   +2 more sources

Substrate Characterization of Bacteroides fragilis α1,3/4-Fucosyltransferase Enabling Access to Programmable One-Pot Enzymatic Synthesis of KH-1 Antigen

, 2019
Bacteroides fragilis α1,3/4-fucosyltransferase (Bf13FT) was expressed in Escherichia coli and characterized as an α1,3/4-fucosyltransferase that can be used as a versatile catalyst for the synthesi...
Hsin-Hui Huang   +9 more
semanticscholar   +1 more source

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