Search results for "Fucose"
showing 8 items of 28 documents
Primary structure and opsonic activity of an F-lectin from serum of the gilt head breamSparus aurata(Pisces, Sparidae)
2012
Abstract The recently described fucose-binding agglutinin from the European eel revealed a novel lectin fold (the ‘F-type’ fold) that is shared with other carbohydrate-binding proteins and proteins from prokaryotes to vertebrates clustered under the newly established F-type lectin (FTL) family. We previously reported the purification and biochemical characterization of a fucose-binding protein (FBP) isolated from serum of the gilt head bream (Sparus aurata, SauFBP). In the present article, the complete coding sequence of SauFBP revealed that it is a member of the FTL family, consisting of two tandem carbohydrate recognition domains (CRD) that display the F-type sequence motif. In vitro opso…
A serum fucolectin isolated and characterized from sea bass Dicentrarchus labrax
2001
A lectin specific for fucose and galactose was isolated by affinity chromatography on Sepharose CL-6B from the serum of Dicentrarchus labrax. The hemagglutinating activity against rabbit erythrocytes was calcium-independent, and reached its maximum at 37 degrees C. Two protein components were found in the hemagglutinating fractions eluted from the Sepharose column. Only the 34 kDa component (DLL2) eluted from the polyacrylamide gels (SDS-PAGE) showed agglutinating activity against rabbit erythrocytes. SDS-PAGE, in non-reducing conditions, revealed a single 66 kDa protein that reacted with antibodies to the 34 kDa component. Therefore, a dimeric structure stabilized by disulfide bonds can be…
Characterization of a proteinaceous extracellular coat synthesized by the ?slime? variant of Neurospora crassa
1989
Cells of the “slime” strain of Neurospora crassa synthesize a coherent extracellular material which remains attached to the cell surface, but is released into the liquid medium by shaking. The material was purified and studied by different criteria. By electron microscopy it appears as long wavy sheets which strongly bind concanavalin A, but not wheat germ agglutinin, and maintain their integrity in the absence of structural polysaccharides. Analysis of the purified material revealed that it was free of contaminating membranes; it contained more than 70% protein, 1% neutral sugars (glucose, mannose, fucose and galactose), less than 2% lipids and ca. 4% not-characterized hexosaminelike compo…
ChemInform Abstract: Synthesis of α-Fucosyl Glycosides and Disaccharides Using 4- Methoxybenzyl (Mpm) Protected Fucosyl Donors.
2010
The 4-methoxybenzyl (Mpm) group removable by selective oxidation was applied as a nonneighbouring-group-active protection of fucose hydroxy functions in the stereoselective synthesis of α-fucosides of acceptors containing double bonds sensitive to hydrogenation. With this aim, the synthesis of the α-fucosyl chloride (4) carrying the acidsensitive Mpm protection was elaborated.
Synthesis of ?-fucosyl glycosides and disaccharides using 4-methoxybenzyl (Mpm) protected fucosyl donors
1992
The 4-methoxybenzyl (Mpm) group removable by selective oxidation was applied as a nonneighbouring-group-active protection of fucose hydroxy functions in the stereoselective synthesis of α-fucosides of acceptors containing double bonds sensitive to hydrogenation. With this aim, the synthesis of the α-fucosyl chloride (4) carrying the acidsensitive Mpm protection was elaborated.
F-Type Lectins: A highly diversified family of fucose-binding proteins with a unique sequence motif and structural fold, involved in self/non-self-re…
2017
The F-type lectin (FTL) family is one of the most recent to be identified and structurally characterized. Members of the FTL family are characterized by a fucose recognition domain [F-type lectin domain (FTLD)] that displays a novel jellyroll fold (“F-type” fold) and unique carbohydrate- and calcium-binding sequence motifs. This novel lectin family comprises widely distributed proteins exhibiting single, double, or greater multiples of the FTLD, either tandemly arrayed or combined with other structurally and functionally distinct domains, yielding lectin subunits of pleiotropic properties even within a single species. Furthermore, the extraordinary variability of FTL sequences (isoforms) th…