Cysteine conjugate β-lyase activity in three species of parasitic helminth
- 作者：Adcock ; Harriet J. ; Brophy ; Peter M. ; Teesdale-Spittle ; Paul H. ; Buckberry ; Lorraine D.
- 关键词：Cysteine conjugate β ; -lyase ; Glutathione S-transferase ; Transaminase ; Parasitic helminth
- 刊名：International Journal for Parasitology
- 出版年：1999
- 期刊代码：124_00207519
- 类别：med
- 出版时间：April, 1999
- 卷：29
- 期：4
- 页码：543-548
- 文件大小：108 K
摘要
Living organisms employ a variety of metabolic pathways when detoxifying xenobiotic compounds, including the formation of cysteine S-conjugates via glutathione conjugation. However, cysteine conjugate β-lyase (CCBL) catalysed β-cleavage, of certain cysteine conjugates, is known to cause cytotoxicity. This study represents the first investigation into the expression of CCBL and other associated enzymes in helminth species. A survey of the three major groups of parasitic helminths [cestodes (Moniezia expansa), digeneans (Fasciola hepatica) and nematodes (Necator americanus, Heligmosomoides polygyrus)] has been made. The presence of CCBL enzymes within Moniezia expansa, Necator americanus and Heligmosomoides polygyrus has been established. Each species was screened for γ-glutamyl transpeptidase activity and transaminase activity towards -aspartate, -alanine, -albizziin and -phenylalanine. Aspartate and alanine aminotransferase activity were detected in all four species tested. γ-Glutamyl transpeptidase activity was only detected in Moniezia expansa and Necator americanus.