Chemical Microdetermination of Heparin in Plasma

Pretreatment Procedure for the Microdetermination of Chondroitin Sulfate in Plasma and Urine

“…In blood plasma, GAGs interact with biologically important proteins, including protease inhibitors, coagulation factors, lipoproteins, and complement proteins (7); cells such as lymphocytes (8), monocytes (9), and platelets (10); and the vascular endothelium (11). The presence of GAGs in human plasma has been demonstrated in several reports (12,13); however, the structures and physicochemical properties of these GAGs have not been fully identified and characterized due to their low blood concentration and a general lack of adequate analytical methodology. Problems with recovery from biological samples are particularly evident for structurally complex GAGs, such as heparin and heparan sulfate, which have strong affinity for plasma components.…”

Cellular Binding of Hepatitis C Virus Envelope Glycoprotein E2 Requires Cell Surface Heparan Sulfate

“…Analysis of Cellular Heparan Sulfate Structure and Sulfation-Disaccharide analysis of cell surface heparan sulfate from freeze-dried HepG2 and MOLT-4 cells using was performed using high performance liquid chromatography with post-column fluorescence detection as previously described (44,45). Analysis of kidney and liver heparan sulfate by capillary electrophoresis has been recently described (40).…”

Estimation of the composition of heparin mixtures from various origins using proton nuclear magnetic resonance and multivariate calibration methods

“…The proton signals of the heparin spectra are grouped in three spectral ranges corresponding to the anomeric (5.0-5.7 ppm), the acetamidomethyl (1.9-2.2 ppm) and the sugar ring protons (2.9-4.5 ppm). Although the major signals of the heparin spectra corresponded to the GlcNS6S and IdoA2S residues, hydrogen signals of other minor residues, such as GlcNAc, GlcNS3S6S, IdoA and GlcA also appeared in the spectra producing complex peaks [1,23,25,44]. All these residues are constituents with variable abundance in all the heparins independently of their different origins.…”

“…The identification of the signals was performed according to the assignments published by other authors [23,25,44] on the basis of their chemical shifts and the interpretation of two-dimensional 1 H-NMR spectra. The proton signals of the heparin spectra are grouped in three spectral ranges corresponding to the anomeric (5.0-5.7 ppm), the acetamidomethyl (1.9-2.2 ppm) and the sugar ring protons (2.9-4.5 ppm).…”

“…Therefore, to date, MS has been used for the characterization of short oligosaccharides fragments released by chemical or enzymatic depolymerization previously isolated by chromatographic or electrophoretic steps [20,21,22], and no information regarding the origin of the products was extracted. 1 H nuclear magnetic resonance (NMR) spectroscopy has become a successful technique for characterizing the chemical composition of intact heparin [1,23,24,25] and heparin-derived oligosaccharides [26,27], and for checking the impurities from other GAGs [23,24,28]. In other instances, NMR spectroscopy is being used in food research in the authentication of the quality of products such as wines, fruit juices and jams [29,30,31,32].…”