Abstract
The proton nuclear magnetic resonance (1H-NMR) spectra of chondroitin sulfates (chondroitin, chondroitin 4-sulfate, chondroitin 6-sulfate and dermatan sulfate) have been obtained at 500 MHz and 333 K in deuterium oxide. The J connectivities of sugar ring protons of chondroitin sulfates are revealed by the uses of homonuclear two-dimensional (2D) multiple-relayed-chemical-shift-correlated spectroscopy (multiple-relayed COSY), homonuclear Hartman-Hahn spectroscopy (2D HOH AH A), and multiple-quantum-filtered COSY. Formation of sulfate ester on JV-acetylgalactos-amine hydroxy group causes predictable 0.4–0.6 ppm deshielding of the proton directly attached to the sulfation site. Furthermore, the partial structure of low-sulfated chondroitin sulfate chain isolated from human urinary trypsin inhibitor was determined from the obtained 1H-NMR data.
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