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. Author manuscript; available in PMC: 2022 Jun 2.
Published in final edited form as: Curr Anal Chem. 2005;1(3):223–240. doi: 10.2174/157341105774573929

Fig. (3).

Fig. (3).

(a) The complex ion of a heparin octasulfated hexasaccharide with a synthetic peptide in MALDI-MS analysis, where m and n correspond to the moles of peptide and oligosaccharide, respectively. Heparinase treatment of a decasaecharide (AT-10) with sequence ΔUAp2SGlcNpS6SIdoAp2SGlcNpS6SIdoAp2SGlcNpS6SIdoApGlcNpAc6SGlcApGlcNpS3S6S. Those species assignable to the contaminant are marked (*). (b) Incomplete heparinase I treatment of AT−10. Under the conditions used in this study, heparinase I cleaves a glycosidic linkage containing an 12S; (c) MALDI mass spectrum of AT-10 fragments from exhaustive digestion with heparinase I; (d) MALDI mass spectrum of tagged AT-10 treated with heparinase I shows five fragments: one with molecular mass of 576.7 Da (assignable to 6 D), two tetrasaccharides with molecular mass of 1073.9 (*) and 1154.0 Da, and a mass tagged hexasaccharide with a molecular mass of 1671.4 (mass of 1615.3 plus the mass tag of 56.1). Because the coupling efficiency was ‘90%, also seen is unlabeled hexasaccharide (mass of 1615.1). (Revised from ref. 74); (e) MALDI mass spectrum of the protonated complex of AT-10 with(RG)l9R; (f) Direct MALDI-MS analysis of a synthetic highly sulfated oligosaccharide, sucrose octasulfate, using matrices comprised of room temperature ionic liquids.