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

Harriet J. Adcock, Peter Brophy, Paul H. Teesdale-Spittle, Lorraine D. Buckberry

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)

Abstract

The paper presents the first report of the purification of an invertebrate cysteine conjugate β-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 Mr 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
Original languageEnglish
Pages (from-to)567-571
Number of pages5
JournalInternational Journal for Parasitology
Volume30
Issue number5
DOIs
Publication statusPublished - 15 Apr 2000

Keywords

  • Cysteine conjugate β-lyase
  • Moniezia expansa
  • Parasite

Fingerprint

Dive into the research topics of 'Purification and characterisation of a novel cysteine conjugate β-lyase from the tapeworm Moniezia expansa'. Together they form a unique fingerprint.

Cite this