Clonorchis sinensis: purification and characterization of a cysteine proteinase from adult worms.
1. Adult Clonorchis sinensis, the Chinese liver fluke, is known to migrate to the bile ducts of its mammalian host and cause significant pathology. 2. An acidic, thiol-dependent proteinase with a native mol. wt of approximately 18,500 was purified to homogeneity using ion-exchange chromatography and gel filtration chromatography. By SDS-polyacrylamide gel electrophoresis, the mol. wt of the enzyme was estimated to be 15,000. 3. The enzyme was similar to cathepsin B-like cysteine proteinases based on pH optimum, substrate specificity, and inhibitor sensitivity. 4. Antisera from human clonorchiasis and C. sinensis-infected rabbits reacted in immunoblots with the partially purified proteinase. The C. sinensis proteinase may be useful for serodiagnosis of clonorchiasis.
Song
C Y
CY
Department of Biology, Chung-Ang University, Seoul, Korea.
Dresden
M H
MH
Rege
A A
AA
D000818:Animals; D002401:Cathepsin B / Q000378:metabolism; D002845:Chromatography; D003004:Clonorchis sinensis / Q000201:enzymology*; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D004229:Dithiothreitol / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D015151:Immunoblotting; D008970:Molecular Weight; D011480:Protease Inhibitors / Q000494:pharmacology; D013379:Substrate Specificity
D011480:Protease Inhibitors; D003546:Cysteine Endopeptidases; D002401:Cathepsin B; D004229:Dithiothreitol