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肝素酶Ⅰ对合成的肝素五糖的酶解作用及对其抗Xa因子活性的影响
引用本文:于广利,管华诗,Jawed Fareed.肝素酶Ⅰ对合成的肝素五糖的酶解作用及对其抗Xa因子活性的影响[J].中国海洋大学学报(自然科学版),2001,31(4):529-535.
作者姓名:于广利  管华诗  Jawed Fareed
作者单位:1. 青岛海洋大学海洋药物与食品研究所,
2. Division of Medicinal and Natural Products Chemistry, University of Iowa,
3. Department of Pathology and Pharmacology, Loyola University Medical Center,
基金项目:美国国立健康研究学会NIH(GM38060)基金资助,在美国Iowa大学Robert J. Linhardt实验室完成
摘    要:研究肝素酶Ⅰ(来源于Flavobacterumheparinase,EC4.2.2.7)对人工合成的且含有与抗凝血酶Ⅲ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-HPLC)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Ⅰ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。

关 键 词:肝素酶Ⅰ(HeparinaseⅠ)  合成肝素五糖(SHP)  抗Xa因子活性
文章编号:1001-1862(2001)04-529-07
修稿时间:2000年9月22日

Hydrolysis of Heparinase
Yu Guangli,Guan Huashi Robert J. Linhardt Jawed Fareed.Hydrolysis of Heparinase[J].Periodical of Ocean University of China,2001,31(4):529-535.
Authors:Yu Guangli  Guan Huashi Robert J Linhardt Jawed Fareed
Institution:Yu Guangli 1 Guan Huashi 1 Robert J. Linhardt2 Jawed Fareed3
Abstract: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.
Keywords:heparinase I  synthetic heparin-pentasaccharide (SHP)  anti-factor Xa activity
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