Purification and characterisation of a novel cysteine conjugate β-lyase from the tapeworm Moniezia expansa

被引：4

作者：

Adcock, HJ

Brophy, PM

Teesdale-Spittle, PH

Buckberry, LD

机构：

[1] De Montfort Univ, Dept Chem, Leicester LE1 9BH, Leics, England

[2] Univ Wales, Inst Biol Sci, Aberystwyth SY23 3DA, Dyfed, Wales

来源：

INTERNATIONAL JOURNAL FOR PARASITOLOGY | 2000年 / 30卷 / 05期

基金：

英国惠康基金;

关键词：

cysteine conjugate beta-lyase; Moniezia expansa; parasite;

D O I：

10.1016/S0020-7519(00)00024-2

中图分类号：

R38 [医学寄生虫学]; Q [生物科学];

学科分类号：

07 [理学]; 0710 [生物学]; 09 [农学]; 100103 [病原生物学];

摘要：

The paper presents the first report of the purification of an invertebrate cysteine conjugate beta-lyase (CCBL). CCBL activity was shown to predominate within the cytosolic fraction of tissue from the tapeworm Moniezia expansa. The monomeric cytosolic enzyme was isolated with a M-r of 72 kDa and co-purified with transaminase activity towards L-aspartate. The substrate profile for M. expansa CCBL is different from that of mammalian CCBLs. Exploiting the differences in mammalian and parasite substrate profiles will facilitate the development of helminth targeted conjugates which will not be activated by host (mammalian) CCBLs. (C) 2000 Australian Society for Parasitology Inc. Published by Elsevier Science Ltd. All rights reserved.

引用

页码：567 / 571

页数：5

共 25 条

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[2]

Cysteine conjugate β-lyase activity in three species of parasitic helminth [J].