8-aminopyrene-1-3-6-trisulfonate has been researched along with maltoheptaose* in 2 studies
2 other study(ies) available for 8-aminopyrene-1-3-6-trisulfonate and maltoheptaose
| Article | Year |
|---|---|
Microscale nonreductive release of O-linked glycans for subsequent analysis through MALDI mass spectrometry and capillary electrophoresis.
A new beta-elimination-based procedure has been devised for a microscale release of O-linked oligosaccharides from glycoproteins. Unlike the conventional Carlson degradation, which leads to formation of alditols, the procedure reported here renders the reducing end intact. Conversion of the liberated oligosaccharides to glycosylamines in ammonia medium is followed by the production of the reducing oligosaccharides through the addition of boric acid. The quantitatively generated oligosaccharides with the reducing end can subsequently be derivatized with a fluorophoric reagent for capillary electrophoresis or, alternatively, analyzed through MALDI mass spectrometry. The microscale version of these chemical steps permits us to investigate structurally O-linked oligosaccharides at very low levels. Topics: alpha-Fetoproteins; Ammonia; Animals; Cattle; Electrophoresis, Capillary; Glucans; Glycoproteins; Humans; Indicators and Reagents; Milk, Human; Mucins; Nanotechnology; ortho-Aminobenzoates; Polysaccharides; Pyrenes; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Sterol Esterase | 2001 |
Profiling glycoprotein n-linked oligosaccharide by capillary electrophoresis.
A method for analysis of N-linked oligosaccharides derived from glycoproteins including sialic acid-containing species is presented. It is based on the combination of specific chemical and enzymatic conversions coupled with capillary electrophoretic (CE) separation and laser-induced fluorescence (LIF) detection. Glycoproteins were heat-denatured in the presence of a reducing agent and the N-linked oligosaccharides were released by peptide N-glycosidase (PNGase F; EC3.5.1.52)-catalyzed hydrolysis. The released N-linked oligosaccharides were derivatized with 8-aminopyrene-1,3,6-trisulfonate (APTS) under mild reductive amination conditions in which desialylation and loss of fucose residues are minimized. A model N-linked oligosaccharide, desialylated, galactosylated biantennary, core-substituted with fucose (A2F) was tested for APTS-based derivatization chemistry with excellent recovery of the adduct without losing fucose and neuraminic acid residues. The profiles of heavily sialylated N-linked oligosaccharides derived from fetuin, recombinant human erythropoietin and kallikrein are reported and the data show that the present method produces a high resolution of the N-linked oligosaccharide profile for fingerprinting glycans derived from glycoproteins. Topics: alpha-Fetoproteins; Amidohydrolases; Carbohydrate Sequence; Carbohydrates; Catalysis; Electrophoresis, Capillary; Erythropoietin; Fluorescent Dyes; Glucans; Glycoproteins; Humans; Kallikreins; Maltose; Molecular Sequence Data; Oligosaccharides; Oxidation-Reduction; Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase; Pyrenes; Ribonucleases | 1998 |