Hydrolase and sialyltransferase activities of Trypanosoma cruzi trans-sialidase towards NeuAc-α-2,3-Gal-β-O-PNP

被引：24

作者：

Harrison, JA

Kartha, KPR

Turnbull, WB

Scheuerl, SL

Naismith, JH

Schenkman, S

Field, RA

机构：

[1] Univ St Andrews, Sch Chem, St Andrews KY16 9ST, Fife, Scotland

[2] Escola Paulista Med, Disc Biol Celular, BR-04023062 Sao Paulo, Brazil

来源：

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS | 2001年 / 11卷 / 02期

基金：

英国生物技术与生命科学研究理事会; 英国惠康基金;

关键词：

D O I：

10.1016/S0960-894X(00)00611-9

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

NeuAc-alpha -2,3-Gal-beta -O-PNP has been synthesised and its ability to act as a substrate for the hydrolase and transferase activities of Trypanosoma cruzi trans-sialidase have been investigated. The turn-over of this compound shows marked differences from the behaviour of NeuAc-MU. In addition, distinct differences in the action of T. cruzi trans-sialidase and Clostridium perfringens neuraminidase on NeuAc-alpha -2,3-Gal-beta -O-PNP were apparent. (C) 2001 Elsevier Science Ltd. All rights reserved.

引用

页码：141 / 144

页数：4

共 24 条

[1] THE MECHANISMS OF TRYPANOSOMA-CRUZI INVASION OF MAMMALIAN-CELLS [J].