Liquid Chromatography/Mass Spectrometry Sequencing Approach for Highly Sulfated Heparin-derived Oligosaccharides

Liquid chromatography/mass spectrometry sequencing approach for highly sulfated heparin-derived oligosaccharides.

Liquid chromatography/mass spectrometry (LC/MS) is applied to the analysis of complex mixtures of oligosaccharides obtained through the controlled, heparinase-catalyzed depolymerization of heparin. Reversed-phase ion-pairing chromatography, utilizing a volatile mobile phase, results in the high resolution separation of highly sulfated, heparin-derived oligosaccharides. Simultaneous detection by...

LC/MS Sequencing Approach for Highly Sulfated Heparin-Derived Oligosaccharides

Capillary Electrophoresis-Mass Spectrometry for the Analysis of Heparin Oligosaccharides and Low Molecular Weight Heparin.

Heparins, highly sulfated, linear polysaccharides also known as glycosaminoglycans, are among the most challenging biopolymers to analyze. Hyphenated techniques in conjunction with mass spectrometry (MS) offer rapid analysis of complex glycosaminoglycan mixtures, providing detailed structural and quantitative data. Previous analytical approaches have often relied on liquid chromatography (LC)-M...

Separation of a complex mixture of heparin-derived oligosaccharides using reversed-phase high-performance liquid chromatography.

A reversed-phase ion-pairing high-performance liquid chromatography (RP-HPIPC) method for the separation of a complex mixture of heparin-derived oligosacchrides has been developed by a stepwise optimization of the mobile phase, in which the concentration of ion-pairing reagent, mobile phase pH, and acetonitrile concentration were varied. The resolution of more than 30 oligosaccharide components...

Heparin sequencing brings structure to the function of complex oligosaccharides.

H is a highly sulfated linear polysaccharide that was discovered in 1916 as an anticoagulant and has been used clinically since 1935 (see ref. 1 for review). The anticoagulant activity of heparin results from its binding to the serine protease inhibitor, antithrombin III (ATIII) (2, 3). Heparin binding causes a conformational change in ATIII that results in enhanced inhibition of thrombin and o...