Purification and characterisation of a novel cysteine conjugate beta-lyase from the tapeworm Moniezia expansa.
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.
Adcock
H J
HJ
Department of Chemistry, De Montfort University, The Gateway, Leicester, UK.
Brophy
P M
PM
Teesdale-Spittle
P H
PH
Buckberry
L D
LD
D000818:Animals; D013437:Carbon-Sulfur Lyases / Q000737:chemistry / Q000302:isolation & purification*; D002589:Cestoda / Q000201:enzymology*; D007422:Intestines / Q000469:parasitology; D012756:Sheep / Q000469:parasitology
D013437:Carbon-Sulfur Lyases; C019969:S-alkylcysteine lyase