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Mass Spectrometric Evidence of Heparin Disaccharides for the Catalytic Characterization of A Novel Endolytic Heparinase

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Acta Biochimica et Biophysica Sinica 2004年第12期36卷 840-844页

作者： yapeng chao1,3. shaoxiang xiong2. xiulan cheng1, and {2. {3.* 1institute of microbiology, chinese academy of Sciences, beijing 100080, china 2.enter of Mass Spectrometry, institute of Chemistry, chinese academy of Sciences, beijing 100080, china 3.raduate School of the chinese academy of Sciences, beijing 10003., china institute of microbiology Chinese Academy of SciencesBeijing 100080 China Graduate School of the chinese academy of Sciences{2. 10003. China Center of Mass Spectrometry Institute of Chemistry Chinese Academy of SciencesBeijing 100080 China

Heparinase from different sources can eliminate heparin or/and heparan sulfate into various low-molecular weight heparins with different characteristics. Porcine intestinal mucosa heparin was de- graded into a series of oligosaccharides by a novel heparinase from the species Sphingobacterium. Disaccha- ride components from the digests were separated and purified by ultrafiltration and HPLC. Five major peaks appeared as three types according to their retention time. The mass spectrometry of peak I mainly gave the non-sulfated disaccharide with the mass of 3.9 Da. Peak II and III were indicated as two major monosulfated disaccharides with molecular mass of 417 and 459 Da respectively. Moreover, the peak III represented an N- acetyl disaccharide. Both peak IV and V showed the same mass of 496 Da, hinting that they were disulfate- substituted disaccharides. No trisulfate-substituted disaccharides were detected in the mixture of the heparin digest though they were abundant in the heparin structure. The results revealed that the heparinase might specifically cut the sites with low sulfated domain in heparin.

关键词： electrospray ionization-mass spectrometry heparin disaccharides heparinase high perfor- mance liquid chromatography Sphingobacterium sp.

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