Heparinase I acts on a synthetic heparin pentasaccharide corresponding to the antithrombin III binding site

被引：46

作者：

Yu, GL

LeBrun, L

Gunay, NS

Hoppensteadt, D

Walenga, JM

Fareed, J

Linhardt, RJ

机构：

[1] Univ Iowa, Div Med & Nat Prod Chem, Iowa City, IA 52242 USA

[2] Univ Iowa, Dept Chem & Biochem Engn, Iowa City, IA 52242 USA

[3] Univ Iowa, Dept Chem, Iowa City, IA 52242 USA

[4] Loyola Univ, Med Ctr, Dept Pharmacol, Maywood, IL 60153 USA

[5] Loyola Univ, Med Ctr, Dept Pathol, Maywood, IL 60153 USA

来源：

THROMBOSIS RESEARCH | 2000年 / 100卷 / 06期

关键词：

heparinase; heparin lyase; pentasaccharide; neutralization; reversal;

D O I：

10.1016/S0049-3848(00)00368-6

中图分类号：

R5 [内科学];

学科分类号：

1002 ; 100201 ;

摘要：

A synthetic pentasaccharide, containing an intact antithrombin III (ATIII) binding site that is in clinical studies a specific antifactor Xa agent, serves as a substrate for a heparin lyase (heparinase I, EC 4.2.2.7) from Flavobacterium heparinum. Heparinase I, currently being assessed as a heparin reversal agent, also reverses the antifactor Xa activity of this synthetic pentasaccharide by breaking it down to inactive disaccharide and trisaccharide products. (C) 2000 Elsevier Science Ltd. All rights reserved.

引用

页码：549 / 556

页数：8

共 23 条

[1] A MODIFIED URONIC ACID CARBAZOLE REACTION [J].