摘要
研究肝素酶 (来源于 Flavobacterum heparinase,EC4 .2 .2 .7)对人工合成的且含有与抗凝血酶 特定结合位点的肝素五糖 (SHP)的酶解作用 ,并对酶解作用的动力学进行研究。利用强阴离子高效液相色谱 (SAX- HPL C)对酶解混合物进行分离 ,利用质谱 (ESIMS)和核磁共振波谱 (1H- NMR)技术对得到的二糖和三糖的结构进行确证。研究结果表明 ,这种被作为肝素反向试剂的肝素酶 可水解人工所合成的肝素五糖 ,从而使之丧失抗 Xa因子活性。
The hydrolysis of Heparinase I (from Flavobacterium heparinase, EC 4.2.2.7) to synthetic heparin-pentasaccharide (SHP) which contained an antithrombin III binding site was examined. The kinetics of this reaction was studied and the products were separated by strong anion exchange high performance liquid chromatography (SAX-HPLC). The structure of disaccharide and trisaccharide derived from SHP were confirmed by NMR and MS techniques. The experiment results showed that, heparinase I, which currently is used as a heparin reversal agent, can also reverses this synthetic pentasaccharide and make it losing its anti-factor Xa activity.
出处
《青岛海洋大学学报（自然科学版）》
CSCD
北大核心
2001年第4期529-535,共7页
Journal of Ocean University of Qingdao
基金
美国国立健康研究学会NIH(GM380 6 0 )基金资助&&
